---
_id: '14795'
abstract:
- lang: eng
text: Metazoan development relies on the formation and remodeling of cell-cell contacts.
Dynamic reorganization of adhesion receptors and the actomyosin cell cortex in
space and time plays a central role in cell-cell contact formation and maturation.
Nevertheless, how this process is mechanistically achieved when new contacts are
formed remains unclear. Here, by building a biomimetic assay composed of progenitor
cells adhering to supported lipid bilayers functionalized with E-cadherin ectodomains,
we show that cortical F-actin flows, driven by the depletion of myosin-2 at the
cell contact center, mediate the dynamic reorganization of adhesion receptors
and cell cortex at the contact. E-cadherin-dependent downregulation of the small
GTPase RhoA at the forming contact leads to both a depletion of myosin-2 and a
decrease of F-actin at the contact center. At the contact rim, in contrast, myosin-2
becomes enriched by the retraction of bleb-like protrusions, resulting in a cortical
tension gradient from the contact rim to its center. This tension gradient, in
turn, triggers centrifugal F-actin flows, leading to further accumulation of F-actin
at the contact rim and the progressive redistribution of E-cadherin from the contact
center to the rim. Eventually, this combination of actomyosin downregulation and
flows at the contact determines the characteristic molecular organization, with
E-cadherin and F-actin accumulating at the contact rim, where they are needed
to mechanically link the contractile cortices of the adhering cells.
acknowledged_ssus:
- _id: Bio
- _id: PreCl
acknowledgement: "We are grateful to Edwin Munro for their feedback and help with
the single particle analysis. We thank members of the Heisenberg and Loose labs
for their help and feedback on the manuscript, notably Xin Tong for making the PCS2-mCherry-AHPH
plasmid. Finally, we thank the Aquatics and Imaging & Optics facilities of ISTA
for their continuous support, especially Yann Cesbron for assistance with the laser
cutter. This work was supported by an ERC\r\nAdvanced Grant (MECSPEC) to C.-P.H."
article_processing_charge: Yes (via OA deal)
article_type: original
arxiv: 1
author:
- first_name: Feyza N
full_name: Arslan, Feyza N
id: 49DA7910-F248-11E8-B48F-1D18A9856A87
last_name: Arslan
orcid: 0000-0001-5809-9566
- first_name: Edouard B
full_name: Hannezo, Edouard B
id: 3A9DB764-F248-11E8-B48F-1D18A9856A87
last_name: Hannezo
orcid: 0000-0001-6005-1561
- first_name: Jack
full_name: Merrin, Jack
id: 4515C308-F248-11E8-B48F-1D18A9856A87
last_name: Merrin
orcid: 0000-0001-5145-4609
- first_name: Martin
full_name: Loose, Martin
id: 462D4284-F248-11E8-B48F-1D18A9856A87
last_name: Loose
orcid: 0000-0001-7309-9724
- first_name: Carl-Philipp J
full_name: Heisenberg, Carl-Philipp J
id: 39427864-F248-11E8-B48F-1D18A9856A87
last_name: Heisenberg
orcid: 0000-0002-0912-4566
citation:
ama: Arslan FN, Hannezo EB, Merrin J, Loose M, Heisenberg C-PJ. Adhesion-induced
cortical flows pattern E-cadherin-mediated cell contacts. Current Biology.
2024;34(1):171-182.e8. doi:10.1016/j.cub.2023.11.067
apa: Arslan, F. N., Hannezo, E. B., Merrin, J., Loose, M., & Heisenberg, C.-P.
J. (2024). Adhesion-induced cortical flows pattern E-cadherin-mediated cell contacts.
Current Biology. Elsevier. https://doi.org/10.1016/j.cub.2023.11.067
chicago: Arslan, Feyza N, Edouard B Hannezo, Jack Merrin, Martin Loose, and Carl-Philipp
J Heisenberg. “Adhesion-Induced Cortical Flows Pattern E-Cadherin-Mediated Cell
Contacts.” Current Biology. Elsevier, 2024. https://doi.org/10.1016/j.cub.2023.11.067.
ieee: F. N. Arslan, E. B. Hannezo, J. Merrin, M. Loose, and C.-P. J. Heisenberg,
“Adhesion-induced cortical flows pattern E-cadherin-mediated cell contacts,” Current
Biology, vol. 34, no. 1. Elsevier, p. 171–182.e8, 2024.
ista: Arslan FN, Hannezo EB, Merrin J, Loose M, Heisenberg C-PJ. 2024. Adhesion-induced
cortical flows pattern E-cadherin-mediated cell contacts. Current Biology. 34(1),
171–182.e8.
mla: Arslan, Feyza N., et al. “Adhesion-Induced Cortical Flows Pattern E-Cadherin-Mediated
Cell Contacts.” Current Biology, vol. 34, no. 1, Elsevier, 2024, p. 171–182.e8,
doi:10.1016/j.cub.2023.11.067.
short: F.N. Arslan, E.B. Hannezo, J. Merrin, M. Loose, C.-P.J. Heisenberg, Current
Biology 34 (2024) 171–182.e8.
corr_author: '1'
date_created: 2024-01-14T23:00:56Z
date_published: 2024-01-08T00:00:00Z
date_updated: 2025-07-22T14:58:27Z
day: '08'
ddc:
- '570'
department:
- _id: CaHe
- _id: EdHa
- _id: MaLo
- _id: NanoFab
doi: 10.1016/j.cub.2023.11.067
ec_funded: 1
external_id:
arxiv:
- '2410.03589'
file:
- access_level: open_access
checksum: 51220b76d72a614208f84bdbfbaf9b72
content_type: application/pdf
creator: dernst
date_created: 2024-01-16T10:53:31Z
date_updated: 2024-01-16T10:53:31Z
file_id: '14813'
file_name: 2024_CurrentBiology_Arslan.pdf
file_size: 5183861
relation: main_file
success: 1
file_date_updated: 2024-01-16T10:53:31Z
has_accepted_license: '1'
intvolume: ' 34'
issue: '1'
language:
- iso: eng
month: '01'
oa: 1
oa_version: Published Version
page: 171-182.e8
project:
- _id: 260F1432-B435-11E9-9278-68D0E5697425
call_identifier: H2020
grant_number: '742573'
name: Interaction and feedback between cell mechanics and fate specification in
vertebrate gastrulation
publication: Current Biology
publication_identifier:
eissn:
- 1879-0445
issn:
- 0960-9822
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: Adhesion-induced cortical flows pattern E-cadherin-mediated cell contacts
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 34
year: '2024'
...
---
_id: '14834'
abstract:
- lang: eng
text: Bacteria divide by binary fission. The protein machine responsible for this
process is the divisome, a transient assembly of more than 30 proteins in and
on the surface of the cytoplasmic membrane. Together, they constrict the cell
envelope and remodel the peptidoglycan layer to eventually split the cell into
two. For Escherichia coli, most molecular players involved in this process have
probably been identified, but obtaining the quantitative information needed for
a mechanistic understanding can often not be achieved from experiments in vivo
alone. Since the discovery of the Z-ring more than 30 years ago, in vitro reconstitution
experiments have been crucial to shed light on molecular processes normally hidden
in the complex environment of the living cell. In this review, we summarize how
rebuilding the divisome from purified components – or at least parts of it - have
been instrumental to obtain the detailed mechanistic understanding of the bacterial
cell division machinery that we have today.
acknowledgement: We acknowledge members of the Loose laboratory at ISTA for helpful
discussions—in particular M. Kojic for his insightful comments. This work was supported
by the Austrian Science Fund (FWF P34607) to M.L.
article_number: '151380'
article_processing_charge: Yes
article_type: review
author:
- first_name: Philipp
full_name: Radler, Philipp
id: 40136C2A-F248-11E8-B48F-1D18A9856A87
last_name: Radler
orcid: '0000-0001-9198-2182 '
- first_name: Martin
full_name: Loose, Martin
id: 462D4284-F248-11E8-B48F-1D18A9856A87
last_name: Loose
orcid: 0000-0001-7309-9724
citation:
ama: 'Radler P, Loose M. A dynamic duo: Understanding the roles of FtsZ and FtsA
for Escherichia coli cell division through in vitro approaches. European Journal
of Cell Biology. 2024;103(1). doi:10.1016/j.ejcb.2023.151380'
apa: 'Radler, P., & Loose, M. (2024). A dynamic duo: Understanding the roles
of FtsZ and FtsA for Escherichia coli cell division through in vitro approaches.
European Journal of Cell Biology. Elsevier. https://doi.org/10.1016/j.ejcb.2023.151380'
chicago: 'Radler, Philipp, and Martin Loose. “A Dynamic Duo: Understanding the Roles
of FtsZ and FtsA for Escherichia Coli Cell Division through in Vitro Approaches.”
European Journal of Cell Biology. Elsevier, 2024. https://doi.org/10.1016/j.ejcb.2023.151380.'
ieee: 'P. Radler and M. Loose, “A dynamic duo: Understanding the roles of FtsZ and
FtsA for Escherichia coli cell division through in vitro approaches,” European
Journal of Cell Biology, vol. 103, no. 1. Elsevier, 2024.'
ista: 'Radler P, Loose M. 2024. A dynamic duo: Understanding the roles of FtsZ and
FtsA for Escherichia coli cell division through in vitro approaches. European
Journal of Cell Biology. 103(1), 151380.'
mla: 'Radler, Philipp, and Martin Loose. “A Dynamic Duo: Understanding the Roles
of FtsZ and FtsA for Escherichia Coli Cell Division through in Vitro Approaches.”
European Journal of Cell Biology, vol. 103, no. 1, 151380, Elsevier, 2024,
doi:10.1016/j.ejcb.2023.151380.'
short: P. Radler, M. Loose, European Journal of Cell Biology 103 (2024).
date_created: 2024-01-18T08:16:43Z
date_published: 2024-01-12T00:00:00Z
date_updated: 2024-01-23T08:37:13Z
day: '12'
ddc:
- '570'
department:
- _id: MaLo
doi: 10.1016/j.ejcb.2023.151380
external_id:
pmid:
- '38218128'
has_accepted_license: '1'
intvolume: ' 103'
issue: '1'
keyword:
- Cell Biology
- General Medicine
- Histology
- Pathology and Forensic Medicine
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1016/j.ejcb.2023.151380
month: '01'
oa: 1
oa_version: Published Version
pmid: 1
project:
- _id: fc38323b-9c52-11eb-aca3-ff8afb4a011d
grant_number: P34607
name: "Understanding bacterial cell division by in vitro\r\nreconstitution"
publication: European Journal of Cell Biology
publication_identifier:
issn:
- 0171-9335
publication_status: epub_ahead
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: 'A dynamic duo: Understanding the roles of FtsZ and FtsA for Escherichia coli
cell division through in vitro approaches'
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 103
year: '2024'
...
---
_id: '14591'
abstract:
- lang: eng
text: Clathrin-mediated endocytosis (CME) is vital for the regulation of plant growth
and development by controlling plasma membrane protein composition and cargo uptake.
CME relies on the precise recruitment of regulators for vesicle maturation and
release. Homologues of components of mammalian vesicle scission are strong candidates
to be part of the scissin machinery in plants, but the precise roles of these
proteins in this process is not fully understood. Here, we characterised the roles
of Plant Dynamin-Related Proteins 2 (DRP2s) and SH3-domain containing protein
2 (SH3P2), the plant homologue to Dynamins’ recruiters, like Endophilin and Amphiphysin,
in the CME by combining high-resolution imaging of endocytic events in vivo and
characterisation of the purified proteins in vitro. Although DRP2s and SH3P2 arrive
similarly late during CME and physically interact, genetic analysis of the Dsh3p1,2,3
triple-mutant and complementation assays with non-SH3P2-interacting DRP2 variants
suggests that SH3P2 does not directly recruit DRP2s to the site of endocytosis.
These observations imply that despite the presence of many well-conserved endocytic
components, plants have acquired a distinct mechanism for CME. One Sentence Summary
In contrast to predictions based on mammalian systems, plant Dynamin-related proteins
2 are recruited to the site of Clathrin-mediated endocytosis independently of
BAR-SH3 proteins.
acknowledged_ssus:
- _id: EM-Fac
- _id: LifeSc
- _id: Bio
article_processing_charge: No
author:
- first_name: Nataliia
full_name: Gnyliukh, Nataliia
id: 390C1120-F248-11E8-B48F-1D18A9856A87
last_name: Gnyliukh
orcid: 0000-0002-2198-0509
- first_name: Alexander J
full_name: Johnson, Alexander J
id: 46A62C3A-F248-11E8-B48F-1D18A9856A87
last_name: Johnson
orcid: 0000-0002-2739-8843
- first_name: Marie-Kristin
full_name: Nagel, Marie-Kristin
last_name: Nagel
- first_name: Aline
full_name: Monzer, Aline
id: 2DB5D88C-D7B3-11E9-B8FD-7907E6697425
last_name: Monzer
- first_name: Annamaria
full_name: Hlavata, Annamaria
id: 36062FEC-F248-11E8-B48F-1D18A9856A87
last_name: Hlavata
- first_name: Erika
full_name: Isono, Erika
last_name: Isono
- first_name: Martin
full_name: Loose, Martin
id: 462D4284-F248-11E8-B48F-1D18A9856A87
last_name: Loose
orcid: 0000-0001-7309-9724
- first_name: Jiří
full_name: Friml, Jiří
id: 4159519E-F248-11E8-B48F-1D18A9856A87
last_name: Friml
orcid: 0000-0002-8302-7596
citation:
ama: Gnyliukh N, Johnson AJ, Nagel M-K, et al. Role of dynamin-related proteins
2 and SH3P2 in clathrin-mediated endocytosis in plants. bioRxiv. doi:10.1101/2023.10.09.561523
apa: Gnyliukh, N., Johnson, A. J., Nagel, M.-K., Monzer, A., Hlavata, A., Isono,
E., … Friml, J. (n.d.). Role of dynamin-related proteins 2 and SH3P2 in clathrin-mediated
endocytosis in plants. bioRxiv. https://doi.org/10.1101/2023.10.09.561523
chicago: Gnyliukh, Nataliia, Alexander J Johnson, Marie-Kristin Nagel, Aline Monzer,
Annamaria Hlavata, Erika Isono, Martin Loose, and Jiří Friml. “Role of Dynamin-Related
Proteins 2 and SH3P2 in Clathrin-Mediated Endocytosis in Plants.” BioRxiv,
n.d. https://doi.org/10.1101/2023.10.09.561523.
ieee: N. Gnyliukh et al., “Role of dynamin-related proteins 2 and SH3P2 in
clathrin-mediated endocytosis in plants,” bioRxiv. .
ista: Gnyliukh N, Johnson AJ, Nagel M-K, Monzer A, Hlavata A, Isono E, Loose M,
Friml J. Role of dynamin-related proteins 2 and SH3P2 in clathrin-mediated endocytosis
in plants. bioRxiv, 10.1101/2023.10.09.561523.
mla: Gnyliukh, Nataliia, et al. “Role of Dynamin-Related Proteins 2 and SH3P2 in
Clathrin-Mediated Endocytosis in Plants.” BioRxiv, doi:10.1101/2023.10.09.561523.
short: N. Gnyliukh, A.J. Johnson, M.-K. Nagel, A. Monzer, A. Hlavata, E. Isono,
M. Loose, J. Friml, BioRxiv (n.d.).
date_created: 2023-11-22T10:17:49Z
date_published: 2023-10-10T00:00:00Z
date_updated: 2023-12-01T13:51:06Z
day: '10'
department:
- _id: JiFr
- _id: MaLo
- _id: CaBe
doi: 10.1101/2023.10.09.561523
ec_funded: 1
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://www.biorxiv.org/content/10.1101/2023.10.09.561523v2
month: '10'
oa: 1
oa_version: Preprint
project:
- _id: 2564DBCA-B435-11E9-9278-68D0E5697425
call_identifier: H2020
grant_number: '665385'
name: International IST Doctoral Program
publication: bioRxiv
publication_status: submitted
related_material:
record:
- id: '14510'
relation: dissertation_contains
status: public
status: public
title: Role of dynamin-related proteins 2 and SH3P2 in clathrin-mediated endocytosis
in plants
type: preprint
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
year: '2023'
...
---
_id: '13116'
abstract:
- lang: eng
text: 'The emergence of large-scale order in self-organized systems relies on local
interactions between individual components. During bacterial cell division, FtsZ
-- a prokaryotic homologue of the eukaryotic protein tubulin -- polymerizes into
treadmilling filaments that further organize into a cytoskeletal ring. In vitro,
FtsZ filaments can form dynamic chiral assemblies. However, how the active and
passive properties of individual filaments relate to these large-scale self-organized
structures remains poorly understood. Here, we connect single filament properties
with the mesoscopic scale by combining minimal active matter simulations and biochemical
reconstitution experiments. We show that density and flexibility of active chiral
filaments define their global order. At intermediate densities, curved, flexible
filaments organize into chiral rings and polar bands. An effectively nematic organization
dominates for high densities and for straight, mutant filaments with increased
rigidity. Our predicted phase diagram captures these features quantitatively,
demonstrating how the flexibility, density and chirality of active filaments affect
their collective behaviour. Our findings shed light on the fundamental properties
of active chiral matter and explain how treadmilling FtsZ filaments organize during
bacterial cell division. '
acknowledged_ssus:
- _id: Bio
- _id: LifeSc
acknowledgement: 'This work was supported by the European Research Council through
grant ERC 2015-StG-679239 and by the Austrian Science Fund (FWF) StandAlone P34607
to M.L., B. P.M. was also supported by the Kanazawa University WPI- NanoLSI Bio-SPM
collaborative research program. Z.D. has received funding from Doctoral Programme
of the Austrian Academy of Sciences (OeAW): Grant agreement 26360. We thank Jan
Brugues (MPI CBG, Dresden, Germany), Andela Saric (ISTA, Klosterneuburg, Austria),
Daniel Pearce (Uni Geneva, Switzerland) for valuable scientific input and comments
on the manuscript. We are also thankful for the support by the Scientific Service
Units (SSU) of IST Austria through resources provided by the Imaging and Optics
Facility (IOF) and the Lab Support Facility (LSF). '
article_processing_charge: No
author:
- first_name: Zuzana
full_name: Dunajova, Zuzana
id: 4B39F286-F248-11E8-B48F-1D18A9856A87
last_name: Dunajova
- first_name: Batirtze
full_name: Prats Mateu, Batirtze
id: 299FE892-F248-11E8-B48F-1D18A9856A87
last_name: Prats Mateu
- first_name: Philipp
full_name: Radler, Philipp
id: 40136C2A-F248-11E8-B48F-1D18A9856A87
last_name: Radler
orcid: '0000-0001-9198-2182 '
- first_name: Keesiang
full_name: Lim, Keesiang
last_name: Lim
- first_name: Dörte
full_name: Brandis, Dörte
last_name: Brandis
- first_name: Philipp
full_name: Velicky, Philipp
id: 39BDC62C-F248-11E8-B48F-1D18A9856A87
last_name: Velicky
orcid: 0000-0002-2340-7431
- first_name: Johann G
full_name: Danzl, Johann G
id: 42EFD3B6-F248-11E8-B48F-1D18A9856A87
last_name: Danzl
orcid: 0000-0001-8559-3973
- first_name: Richard W.
full_name: Wong, Richard W.
last_name: Wong
- first_name: Jens
full_name: Elgeti, Jens
last_name: Elgeti
- first_name: Edouard B
full_name: Hannezo, Edouard B
id: 3A9DB764-F248-11E8-B48F-1D18A9856A87
last_name: Hannezo
orcid: 0000-0001-6005-1561
- first_name: Martin
full_name: Loose, Martin
id: 462D4284-F248-11E8-B48F-1D18A9856A87
last_name: Loose
orcid: 0000-0001-7309-9724
citation:
ama: Dunajova Z, Prats Mateu B, Radler P, et al. Chiral and nematic phases of flexible
active filaments. 2023. doi:10.15479/AT:ISTA:13116
apa: Dunajova, Z., Prats Mateu, B., Radler, P., Lim, K., Brandis, D., Velicky, P.,
… Loose, M. (2023). Chiral and nematic phases of flexible active filaments. Institute
of Science and Technology Austria. https://doi.org/10.15479/AT:ISTA:13116
chicago: Dunajova, Zuzana, Batirtze Prats Mateu, Philipp Radler, Keesiang Lim, Dörte
Brandis, Philipp Velicky, Johann G Danzl, et al. “Chiral and Nematic Phases of
Flexible Active Filaments.” Institute of Science and Technology Austria, 2023.
https://doi.org/10.15479/AT:ISTA:13116.
ieee: Z. Dunajova et al., “Chiral and nematic phases of flexible active filaments.”
Institute of Science and Technology Austria, 2023.
ista: Dunajova Z, Prats Mateu B, Radler P, Lim K, Brandis D, Velicky P, Danzl JG,
Wong RW, Elgeti J, Hannezo EB, Loose M. 2023. Chiral and nematic phases of flexible
active filaments, Institute of Science and Technology Austria, 10.15479/AT:ISTA:13116.
mla: Dunajova, Zuzana, et al. Chiral and Nematic Phases of Flexible Active Filaments.
Institute of Science and Technology Austria, 2023, doi:10.15479/AT:ISTA:13116.
short: Z. Dunajova, B. Prats Mateu, P. Radler, K. Lim, D. Brandis, P. Velicky, J.G.
Danzl, R.W. Wong, J. Elgeti, E.B. Hannezo, M. Loose, (2023).
date_created: 2023-06-02T12:30:40Z
date_published: 2023-07-26T00:00:00Z
date_updated: 2024-02-21T12:19:09Z
day: '26'
ddc:
- '539'
department:
- _id: MaLo
- _id: EdHa
- _id: JoDa
doi: 10.15479/AT:ISTA:13116
ec_funded: 1
file:
- access_level: open_access
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content_type: application/vnd.openxmlformats-officedocument.wordprocessingml.document
creator: pradler
date_created: 2023-08-08T11:17:28Z
date_updated: 2023-08-08T11:17:28Z
file_id: '13983'
file_name: ReadMe File.docx
file_size: 13111
relation: main_file
success: 1
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content_type: application/octet-stream
creator: pradler
date_created: 2023-07-25T06:55:43Z
date_updated: 2023-07-25T06:55:43Z
file_id: '13298'
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file_size: 1499504777
relation: main_file
success: 1
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content_type: application/octet-stream
creator: pradler
date_created: 2023-07-25T08:31:07Z
date_updated: 2023-07-25T08:31:07Z
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content_type: application/octet-stream
creator: pradler
date_created: 2023-07-25T06:56:54Z
date_updated: 2023-07-25T06:56:54Z
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file_size: 1292391225
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success: 1
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creator: pradler
date_created: 2023-07-25T08:25:07Z
date_updated: 2023-07-25T08:25:07Z
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project:
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call_identifier: H2020
grant_number: '679239'
name: Self-Organization of the Bacterial Cell
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name: Motile active matter models of migrating cells and chiral filaments
publisher: Institute of Science and Technology Austria
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status: public
title: Chiral and nematic phases of flexible active filaments
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image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: research_data
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
year: '2023'
...
---
_id: '13314'
abstract:
- lang: eng
text: The emergence of large-scale order in self-organized systems relies on local
interactions between individual components. During bacterial cell division, FtsZ—a
prokaryotic homologue of the eukaryotic protein tubulin—polymerizes into treadmilling
filaments that further organize into a cytoskeletal ring. In vitro, FtsZ filaments
can form dynamic chiral assemblies. However, how the active and passive properties
of individual filaments relate to these large-scale self-organized structures
remains poorly understood. Here we connect single-filament properties with the
mesoscopic scale by combining minimal active matter simulations and biochemical
reconstitution experiments. We show that the density and flexibility of active
chiral filaments define their global order. At intermediate densities, curved,
flexible filaments organize into chiral rings and polar bands. An effectively
nematic organization dominates for high densities and for straight, mutant filaments
with increased rigidity. Our predicted phase diagram quantitatively captures these
features, demonstrating how the flexibility, density and chirality of the active
filaments affect their collective behaviour. Our findings shed light on the fundamental
properties of active chiral matter and explain how treadmilling FtsZ filaments
organize during bacterial cell division.
acknowledged_ssus:
- _id: Bio
- _id: LifeSc
acknowledgement: 'This work was supported by the European Research Council through
grant ERC 2015-StG-679239 and by the Austrian Science Fund (FWF) StandAlone P34607
to M.L., B. P.M. was also supported by the Kanazawa University WPI- NanoLSI Bio-SPM
collaborative research program. Z.D. has received funding from Doctoral Programme
of the Austrian Academy of Sciences (OeAW): Grant agreement 26360. We thank Jan
Brugues (MPI CBG, Dresden, Germany), Andela Saric (ISTA, Klosterneuburg, Austria),
Daniel Pearce (Uni Geneva, Switzerland) for valuable scientific input and comments
on the manuscript. We are also thankful for the support by the Scientific Service
Units (SSU) of IST Austria through resources provided by the Imaging and Optics
Facility (IOF) and the Lab Support Facility (LSF).'
article_processing_charge: Yes (in subscription journal)
article_type: original
author:
- first_name: Zuzana
full_name: Dunajova, Zuzana
id: 4B39F286-F248-11E8-B48F-1D18A9856A87
last_name: Dunajova
- first_name: Batirtze
full_name: Prats Mateu, Batirtze
id: 299FE892-F248-11E8-B48F-1D18A9856A87
last_name: Prats Mateu
- first_name: Philipp
full_name: Radler, Philipp
id: 40136C2A-F248-11E8-B48F-1D18A9856A87
last_name: Radler
orcid: '0000-0001-9198-2182 '
- first_name: Keesiang
full_name: Lim, Keesiang
last_name: Lim
- first_name: Dörte
full_name: Brandis, Dörte
id: 21d64d35-f128-11eb-9611-b8bcca7a12fd
last_name: Brandis
- first_name: Philipp
full_name: Velicky, Philipp
id: 39BDC62C-F248-11E8-B48F-1D18A9856A87
last_name: Velicky
orcid: 0000-0002-2340-7431
- first_name: Johann G
full_name: Danzl, Johann G
id: 42EFD3B6-F248-11E8-B48F-1D18A9856A87
last_name: Danzl
orcid: 0000-0001-8559-3973
- first_name: Richard W.
full_name: Wong, Richard W.
last_name: Wong
- first_name: Jens
full_name: Elgeti, Jens
last_name: Elgeti
- first_name: Edouard B
full_name: Hannezo, Edouard B
id: 3A9DB764-F248-11E8-B48F-1D18A9856A87
last_name: Hannezo
orcid: 0000-0001-6005-1561
- first_name: Martin
full_name: Loose, Martin
id: 462D4284-F248-11E8-B48F-1D18A9856A87
last_name: Loose
orcid: 0000-0001-7309-9724
citation:
ama: Dunajova Z, Prats Mateu B, Radler P, et al. Chiral and nematic phases of flexible
active filaments. Nature Physics. 2023;19:1916-1926. doi:10.1038/s41567-023-02218-w
apa: Dunajova, Z., Prats Mateu, B., Radler, P., Lim, K., Brandis, D., Velicky, P.,
… Loose, M. (2023). Chiral and nematic phases of flexible active filaments. Nature
Physics. Springer Nature. https://doi.org/10.1038/s41567-023-02218-w
chicago: Dunajova, Zuzana, Batirtze Prats Mateu, Philipp Radler, Keesiang Lim, Dörte
Brandis, Philipp Velicky, Johann G Danzl, et al. “Chiral and Nematic Phases of
Flexible Active Filaments.” Nature Physics. Springer Nature, 2023. https://doi.org/10.1038/s41567-023-02218-w.
ieee: Z. Dunajova et al., “Chiral and nematic phases of flexible active filaments,”
Nature Physics, vol. 19. Springer Nature, pp. 1916–1926, 2023.
ista: Dunajova Z, Prats Mateu B, Radler P, Lim K, Brandis D, Velicky P, Danzl JG,
Wong RW, Elgeti J, Hannezo EB, Loose M. 2023. Chiral and nematic phases of flexible
active filaments. Nature Physics. 19, 1916–1926.
mla: Dunajova, Zuzana, et al. “Chiral and Nematic Phases of Flexible Active Filaments.”
Nature Physics, vol. 19, Springer Nature, 2023, pp. 1916–26, doi:10.1038/s41567-023-02218-w.
short: Z. Dunajova, B. Prats Mateu, P. Radler, K. Lim, D. Brandis, P. Velicky, J.G.
Danzl, R.W. Wong, J. Elgeti, E.B. Hannezo, M. Loose, Nature Physics 19 (2023)
1916–1926.
date_created: 2023-07-27T14:44:45Z
date_published: 2023-12-01T00:00:00Z
date_updated: 2024-02-21T12:19:08Z
day: '01'
ddc:
- '530'
department:
- _id: JoDa
- _id: EdHa
- _id: MaLo
- _id: GradSch
doi: 10.1038/s41567-023-02218-w
ec_funded: 1
external_id:
pmid:
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page: 1916-1926
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project:
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call_identifier: H2020
grant_number: '679239'
name: Self-Organization of the Bacterial Cell
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name: Motile active matter models of migrating cells and chiral filaments
publication: Nature Physics
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title: Chiral and nematic phases of flexible active filaments
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 19
year: '2023'
...
---
_id: '14039'
abstract:
- lang: eng
text: Membranes are essential for life. They act as semi-permeable boundaries that
define cells and organelles. In addition, their surfaces actively participate
in biochemical reaction networks, where they confine proteins, align reaction
partners, and directly control enzymatic activities. Membrane-localized reactions
shape cellular membranes, define the identity of organelles, compartmentalize
biochemical processes, and can even be the source of signaling gradients that
originate at the plasma membrane and reach into the cytoplasm and nucleus. The
membrane surface is, therefore, an essential platform upon which myriad cellular
processes are scaffolded. In this review, we summarize our current understanding
of the biophysics and biochemistry of membrane-localized reactions with particular
focus on insights derived from reconstituted and cellular systems. We discuss
how the interplay of cellular factors results in their self-organization, condensation,
assembly, and activity, and the emergent properties derived from them.
acknowledgement: We acknowledge funding from the Austrian Science Fund (FWF F79, P32814-B,
and P35061-B to S.M.; P34607-B to M.L.; and P30584-B and P33066-B to T.A.L.) and
the European Research Council (ERC) under the European Union’s Horizon 2020 research
and innovation program (grant agreement no. 101045340 to M.L.). We are grateful
for comments on the manuscript by Justyna Sawa-Makarska, Verena Baumann, Marko Kojic,
Philipp Radler, Ronja Reinhardt, and Sumire Antonioli.
article_processing_charge: Yes (via OA deal)
article_type: original
author:
- first_name: Thomas A.
full_name: Leonard, Thomas A.
last_name: Leonard
- first_name: Martin
full_name: Loose, Martin
id: 462D4284-F248-11E8-B48F-1D18A9856A87
last_name: Loose
orcid: 0000-0001-7309-9724
- first_name: Sascha
full_name: Martens, Sascha
last_name: Martens
citation:
ama: Leonard TA, Loose M, Martens S. The membrane surface as a platform that organizes
cellular and biochemical processes. Developmental Cell. 2023;58(15):1315-1332.
doi:10.1016/j.devcel.2023.06.001
apa: Leonard, T. A., Loose, M., & Martens, S. (2023). The membrane surface as
a platform that organizes cellular and biochemical processes. Developmental
Cell. Elsevier. https://doi.org/10.1016/j.devcel.2023.06.001
chicago: Leonard, Thomas A., Martin Loose, and Sascha Martens. “The Membrane Surface
as a Platform That Organizes Cellular and Biochemical Processes.” Developmental
Cell. Elsevier, 2023. https://doi.org/10.1016/j.devcel.2023.06.001.
ieee: T. A. Leonard, M. Loose, and S. Martens, “The membrane surface as a platform
that organizes cellular and biochemical processes,” Developmental Cell,
vol. 58, no. 15. Elsevier, pp. 1315–1332, 2023.
ista: Leonard TA, Loose M, Martens S. 2023. The membrane surface as a platform that
organizes cellular and biochemical processes. Developmental Cell. 58(15), 1315–1332.
mla: Leonard, Thomas A., et al. “The Membrane Surface as a Platform That Organizes
Cellular and Biochemical Processes.” Developmental Cell, vol. 58, no. 15,
Elsevier, 2023, pp. 1315–32, doi:10.1016/j.devcel.2023.06.001.
short: T.A. Leonard, M. Loose, S. Martens, Developmental Cell 58 (2023) 1315–1332.
date_created: 2023-08-13T22:01:12Z
date_published: 2023-08-07T00:00:00Z
date_updated: 2023-12-13T12:09:20Z
day: '07'
ddc:
- '570'
department:
- _id: MaLo
doi: 10.1016/j.devcel.2023.06.001
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isi:
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page: 1315-1332
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project:
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grant_number: P34607
name: "Understanding bacterial cell division by in vitro\r\nreconstitution"
- _id: bd6ae2ca-d553-11ed-ba76-a4aa239da5ee
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name: Synthetic and structural biology of Rab GTPase networks
publication: Developmental Cell
publication_identifier:
eissn:
- 1878-1551
issn:
- 1534-5807
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: The membrane surface as a platform that organizes cellular and biochemical
processes
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 58
year: '2023'
...
---
_id: '12163'
abstract:
- lang: eng
text: Small GTPases play essential roles in the organization of eukaryotic cells.
In recent years, it has become clear that their intracellular functions result
from intricate biochemical networks of the GTPase and their regulators that dynamically
bind to a membrane surface. Due to the inherent complexities of their interactions,
however, revealing the underlying mechanisms of action is often difficult to achieve
from in vivo studies. This review summarizes in vitro reconstitution approaches
developed to obtain a better mechanistic understanding of how small GTPase activities
are regulated in space and time.
acknowledgement: The authors acknowledge support from IST Austria and helpful comments
from the anonymous reviewers that helped to improve this manuscript. We apologize
to the authors of primary literature and outstanding research not cited here due
to space restraints.
article_processing_charge: Yes (via OA deal)
article_type: review
author:
- first_name: Martin
full_name: Loose, Martin
id: 462D4284-F248-11E8-B48F-1D18A9856A87
last_name: Loose
orcid: 0000-0001-7309-9724
- first_name: Albert
full_name: Auer, Albert
id: 3018E8C2-F248-11E8-B48F-1D18A9856A87
last_name: Auer
orcid: 0000-0002-3580-2906
- first_name: Gabriel
full_name: Brognara, Gabriel
id: D96FFDA0-A884-11E9-9968-DC26E6697425
last_name: Brognara
- first_name: Hanifatul R
full_name: Budiman, Hanifatul R
id: 55380f95-15b2-11ec-abd3-aff8e230696b
last_name: Budiman
- first_name: Lukasz M
full_name: Kowalski, Lukasz M
id: e3a512e2-4bbe-11eb-a68a-e3857a7844c2
last_name: Kowalski
- first_name: Ivana
full_name: Matijevic, Ivana
id: 83c17ce3-15b2-11ec-abd3-f486545870bd
last_name: Matijevic
citation:
ama: Loose M, Auer A, Brognara G, Budiman HR, Kowalski LM, Matijevic I. In vitro
reconstitution of small GTPase regulation. FEBS Letters. 2023;597(6):762-777.
doi:10.1002/1873-3468.14540
apa: Loose, M., Auer, A., Brognara, G., Budiman, H. R., Kowalski, L. M., & Matijevic,
I. (2023). In vitro reconstitution of small GTPase regulation. FEBS Letters.
Wiley. https://doi.org/10.1002/1873-3468.14540
chicago: Loose, Martin, Albert Auer, Gabriel Brognara, Hanifatul R Budiman, Lukasz
M Kowalski, and Ivana Matijevic. “In Vitro Reconstitution of Small GTPase Regulation.”
FEBS Letters. Wiley, 2023. https://doi.org/10.1002/1873-3468.14540.
ieee: M. Loose, A. Auer, G. Brognara, H. R. Budiman, L. M. Kowalski, and I. Matijevic,
“In vitro reconstitution of small GTPase regulation,” FEBS Letters, vol.
597, no. 6. Wiley, pp. 762–777, 2023.
ista: Loose M, Auer A, Brognara G, Budiman HR, Kowalski LM, Matijevic I. 2023. In
vitro reconstitution of small GTPase regulation. FEBS Letters. 597(6), 762–777.
mla: Loose, Martin, et al. “In Vitro Reconstitution of Small GTPase Regulation.”
FEBS Letters, vol. 597, no. 6, Wiley, 2023, pp. 762–77, doi:10.1002/1873-3468.14540.
short: M. Loose, A. Auer, G. Brognara, H.R. Budiman, L.M. Kowalski, I. Matijevic,
FEBS Letters 597 (2023) 762–777.
date_created: 2023-01-12T12:09:58Z
date_published: 2023-03-01T00:00:00Z
date_updated: 2023-08-16T08:32:29Z
day: '01'
ddc:
- '570'
department:
- _id: MaLo
doi: 10.1002/1873-3468.14540
external_id:
isi:
- '000891573000001'
pmid:
- '36448231'
file:
- access_level: open_access
checksum: 7492244d3f9c5faa1347ef03f6e5bc84
content_type: application/pdf
creator: dernst
date_created: 2023-08-16T08:31:04Z
date_updated: 2023-08-16T08:31:04Z
file_id: '14063'
file_name: 2023_FEBSLetters_Loose.pdf
file_size: 3148143
relation: main_file
success: 1
file_date_updated: 2023-08-16T08:31:04Z
has_accepted_license: '1'
intvolume: ' 597'
isi: 1
issue: '6'
keyword:
- Cell Biology
- Genetics
- Molecular Biology
- Biochemistry
- Structural Biology
- Biophysics
language:
- iso: eng
month: '03'
oa: 1
oa_version: Published Version
page: 762-777
pmid: 1
publication: FEBS Letters
publication_identifier:
eissn:
- 1873-3468
issn:
- 0014-5793
publication_status: published
publisher: Wiley
quality_controlled: '1'
scopus_import: '1'
status: public
title: In vitro reconstitution of small GTPase regulation
tmp:
image: /images/cc_by_nc_nd.png
legal_code_url: https://creativecommons.org/licenses/by-nc-nd/4.0/legalcode
name: Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International
(CC BY-NC-ND 4.0)
short: CC BY-NC-ND (4.0)
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 597
year: '2023'
...
---
_id: '11373'
abstract:
- lang: eng
text: The actin-homologue FtsA is essential for E. coli cell division, as it links
FtsZ filaments in the Z-ring to transmembrane proteins. FtsA is thought to initiate
cell constriction by switching from an inactive polymeric to an active monomeric
conformation, which recruits downstream proteins and stabilizes the Z-ring. However,
direct biochemical evidence for this mechanism is missing. Here, we use reconstitution
experiments and quantitative fluorescence microscopy to study divisome activation
in vitro. By comparing wild-type FtsA with FtsA R286W, we find that this hyperactive
mutant outperforms FtsA WT in replicating FtsZ treadmilling dynamics, FtsZ filament
stabilization and recruitment of FtsN. We could attribute these differences to
a faster exchange and denser packing of FtsA R286W below FtsZ filaments. Using
FRET microscopy, we also find that FtsN binding promotes FtsA self-interaction.
We propose that in the active divisome FtsA and FtsN exist as a dynamic copolymer
that follows treadmilling filaments of FtsZ.
acknowledged_ssus:
- _id: Bio
- _id: LifeSc
acknowledgement: We acknowledge members of the Loose laboratory at IST Austria for
helpful discussions—in particular L. Lindorfer for his assistance with cloning and
purifications. We thank J. Löwe and T. Nierhaus (MRC-LMB Cambridge, UK) for sharing
unpublished work and helpful discussions, as well as D. Vavylonis and D. Rutkowski
(Lehigh University, Bethlehem, PA, USA) and S. Martin (University of Lausanne, Switzerland)
for sharing their code for FRAP analysis. We are also thankful for the support by
the Scientific Service Units (SSU) of IST Austria through resources provided by
the Imaging and Optics Facility (IOF) and the Lab Support Facility (LSF). This work
was supported by the European Research Council through grant ERC 2015-StG-679239
and by the Austrian Science Fund (FWF) StandAlone P34607 to M.L. and HFSP LT 000824/2016-L4
to N.B. For the purpose of open access, we have applied a CC BY public copyright
licence to any Author Accepted Manuscript version arising from this submission.
article_number: '2635'
article_processing_charge: No
article_type: original
author:
- first_name: Philipp
full_name: Radler, Philipp
id: 40136C2A-F248-11E8-B48F-1D18A9856A87
last_name: Radler
orcid: '0000-0001-9198-2182 '
- first_name: Natalia S.
full_name: Baranova, Natalia S.
id: 38661662-F248-11E8-B48F-1D18A9856A87
last_name: Baranova
orcid: 0000-0002-3086-9124
- first_name: Paulo R
full_name: Dos Santos Caldas, Paulo R
id: 38FCDB4C-F248-11E8-B48F-1D18A9856A87
last_name: Dos Santos Caldas
orcid: 0000-0001-6730-4461
- first_name: Christoph M
full_name: Sommer, Christoph M
id: 4DF26D8C-F248-11E8-B48F-1D18A9856A87
last_name: Sommer
orcid: 0000-0003-1216-9105
- first_name: Maria D
full_name: Lopez Pelegrin, Maria D
id: 319AA9CE-F248-11E8-B48F-1D18A9856A87
last_name: Lopez Pelegrin
- first_name: David
full_name: Michalik, David
id: B9577E20-AA38-11E9-AC9A-0930E6697425
last_name: Michalik
- first_name: Martin
full_name: Loose, Martin
id: 462D4284-F248-11E8-B48F-1D18A9856A87
last_name: Loose
orcid: 0000-0001-7309-9724
citation:
ama: Radler P, Baranova NS, Dos Santos Caldas PR, et al. In vitro reconstitution
of Escherichia coli divisome activation. Nature Communications. 2022;13.
doi:10.1038/s41467-022-30301-y
apa: Radler, P., Baranova, N. S., Dos Santos Caldas, P. R., Sommer, C. M., Lopez
Pelegrin, M. D., Michalik, D., & Loose, M. (2022). In vitro reconstitution
of Escherichia coli divisome activation. Nature Communications. Springer
Nature. https://doi.org/10.1038/s41467-022-30301-y
chicago: Radler, Philipp, Natalia S. Baranova, Paulo R Dos Santos Caldas, Christoph
M Sommer, Maria D Lopez Pelegrin, David Michalik, and Martin Loose. “In Vitro
Reconstitution of Escherichia Coli Divisome Activation.” Nature Communications.
Springer Nature, 2022. https://doi.org/10.1038/s41467-022-30301-y.
ieee: P. Radler et al., “In vitro reconstitution of Escherichia coli divisome
activation,” Nature Communications, vol. 13. Springer Nature, 2022.
ista: Radler P, Baranova NS, Dos Santos Caldas PR, Sommer CM, Lopez Pelegrin MD,
Michalik D, Loose M. 2022. In vitro reconstitution of Escherichia coli divisome
activation. Nature Communications. 13, 2635.
mla: Radler, Philipp, et al. “In Vitro Reconstitution of Escherichia Coli Divisome
Activation.” Nature Communications, vol. 13, 2635, Springer Nature, 2022,
doi:10.1038/s41467-022-30301-y.
short: P. Radler, N.S. Baranova, P.R. Dos Santos Caldas, C.M. Sommer, M.D. Lopez
Pelegrin, D. Michalik, M. Loose, Nature Communications 13 (2022).
date_created: 2022-05-13T09:06:28Z
date_published: 2022-05-12T00:00:00Z
date_updated: 2024-02-21T12:35:18Z
day: '12'
ddc:
- '570'
department:
- _id: MaLo
doi: 10.1038/s41467-022-30301-y
ec_funded: 1
external_id:
isi:
- '000795171100037'
file:
- access_level: open_access
checksum: 5af863ee1b95a0710f6ee864d68dc7a6
content_type: application/pdf
creator: dernst
date_created: 2022-05-13T09:10:51Z
date_updated: 2022-05-13T09:10:51Z
file_id: '11374'
file_name: 2022_NatureCommunications_Radler.pdf
file_size: 6945191
relation: main_file
success: 1
file_date_updated: 2022-05-13T09:10:51Z
has_accepted_license: '1'
intvolume: ' 13'
isi: 1
keyword:
- General Physics and Astronomy
- General Biochemistry
- Genetics and Molecular Biology
- General Chemistry
language:
- iso: eng
month: '05'
oa: 1
oa_version: Published Version
project:
- _id: 2595697A-B435-11E9-9278-68D0E5697425
call_identifier: H2020
grant_number: '679239'
name: Self-Organization of the Bacterial Cell
- _id: fc38323b-9c52-11eb-aca3-ff8afb4a011d
grant_number: P34607
name: "Understanding bacterial cell division by in vitro\r\nreconstitution"
publication: Nature Communications
publication_identifier:
issn:
- 2041-1723
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
related_material:
link:
- relation: erratum
url: https://doi.org/10.1038/s41467-022-34485-1
record:
- id: '14280'
relation: dissertation_contains
status: public
- id: '10934'
relation: research_data
status: public
scopus_import: '1'
status: public
title: In vitro reconstitution of Escherichia coli divisome activation
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 13
year: '2022'
...
---
_id: '8988'
abstract:
- lang: eng
text: The differentiation of cells depends on a precise control of their internal
organization, which is the result of a complex dynamic interplay between the cytoskeleton,
molecular motors, signaling molecules, and membranes. For example, in the developing
neuron, the protein ADAP1 (ADP-ribosylation factor GTPase-activating protein [ArfGAP]
with dual pleckstrin homology [PH] domains 1) has been suggested to control dendrite
branching by regulating the small GTPase ARF6. Together with the motor protein
KIF13B, ADAP1 is also thought to mediate delivery of the second messenger phosphatidylinositol
(3,4,5)-trisphosphate (PIP3) to the axon tip, thus contributing to PIP3 polarity.
However, what defines the function of ADAP1 and how its different roles are coordinated
are still not clear. Here, we studied ADAP1’s functions using in vitro reconstitutions.
We found that KIF13B transports ADAP1 along microtubules, but that PIP3 as well
as PI(3,4)P2 act as stop signals for this transport instead of being transported.
We also demonstrate that these phosphoinositides activate ADAP1’s enzymatic activity
to catalyze GTP hydrolysis by ARF6. Together, our results support a model for
the cellular function of ADAP1, where KIF13B transports ADAP1 until it encounters
high PIP3/PI(3,4)P2 concentrations in the plasma membrane. Here, ADAP1 disassociates
from the motor to inactivate ARF6, promoting dendrite branching.
acknowledged_ssus:
- _id: Bio
- _id: LifeSc
- _id: EM-Fac
acknowledgement: "We thank Urban Bezeljak, Natalia Baranova, Mar Lopez-Pelegrin, Catarina
Alcarva, and Victoria Faas for sharing reagents and helpful discussions. We thank
Veronika Szentirmai for help with protein purifications. We thank Carrie Bernecky,
Sascha Martens, and the M.L. lab for comments on the manuscript. We thank the bioimaging
facility, the life science facility, and Armel Nicolas from the mass spec facility
at the Institute of Science and Technology (IST) Austria for technical support.
C.D. acknowledges funding from the IST fellowship program; this work was supported
by Human Frontier Science Program Young Investigator Grant\r\nRGY0083/2016. "
article_number: e2010054118
article_processing_charge: No
article_type: original
author:
- first_name: Christian F
full_name: Düllberg, Christian F
id: 459064DC-F248-11E8-B48F-1D18A9856A87
last_name: Düllberg
orcid: 0000-0001-6335-9748
- first_name: Albert
full_name: Auer, Albert
id: 3018E8C2-F248-11E8-B48F-1D18A9856A87
last_name: Auer
orcid: 0000-0002-3580-2906
- first_name: Nikola
full_name: Canigova, Nikola
id: 3795523E-F248-11E8-B48F-1D18A9856A87
last_name: Canigova
orcid: 0000-0002-8518-5926
- first_name: Katrin
full_name: Loibl, Katrin
id: 3760F32C-F248-11E8-B48F-1D18A9856A87
last_name: Loibl
orcid: 0000-0002-2429-7668
- first_name: Martin
full_name: Loose, Martin
id: 462D4284-F248-11E8-B48F-1D18A9856A87
last_name: Loose
orcid: 0000-0001-7309-9724
citation:
ama: Düllberg CF, Auer A, Canigova N, Loibl K, Loose M. In vitro reconstitution
reveals phosphoinositides as cargo-release factors and activators of the ARF6
GAP ADAP1. PNAS. 2021;118(1). doi:10.1073/pnas.2010054118
apa: Düllberg, C. F., Auer, A., Canigova, N., Loibl, K., & Loose, M. (2021).
In vitro reconstitution reveals phosphoinositides as cargo-release factors and
activators of the ARF6 GAP ADAP1. PNAS. National Academy of Sciences. https://doi.org/10.1073/pnas.2010054118
chicago: Düllberg, Christian F, Albert Auer, Nikola Canigova, Katrin Loibl, and
Martin Loose. “In Vitro Reconstitution Reveals Phosphoinositides as Cargo-Release
Factors and Activators of the ARF6 GAP ADAP1.” PNAS. National Academy of
Sciences, 2021. https://doi.org/10.1073/pnas.2010054118.
ieee: C. F. Düllberg, A. Auer, N. Canigova, K. Loibl, and M. Loose, “In vitro reconstitution
reveals phosphoinositides as cargo-release factors and activators of the ARF6
GAP ADAP1,” PNAS, vol. 118, no. 1. National Academy of Sciences, 2021.
ista: Düllberg CF, Auer A, Canigova N, Loibl K, Loose M. 2021. In vitro reconstitution
reveals phosphoinositides as cargo-release factors and activators of the ARF6
GAP ADAP1. PNAS. 118(1), e2010054118.
mla: Düllberg, Christian F., et al. “In Vitro Reconstitution Reveals Phosphoinositides
as Cargo-Release Factors and Activators of the ARF6 GAP ADAP1.” PNAS, vol.
118, no. 1, e2010054118, National Academy of Sciences, 2021, doi:10.1073/pnas.2010054118.
short: C.F. Düllberg, A. Auer, N. Canigova, K. Loibl, M. Loose, PNAS 118 (2021).
date_created: 2021-01-03T23:01:23Z
date_published: 2021-01-05T00:00:00Z
date_updated: 2023-08-04T11:20:46Z
day: '05'
department:
- _id: MaLo
- _id: MiSi
doi: 10.1073/pnas.2010054118
external_id:
isi:
- '000607270100018'
pmid:
- '33443153'
intvolume: ' 118'
isi: 1
issue: '1'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1073/pnas.2010054118
month: '01'
oa: 1
oa_version: Published Version
pmid: 1
project:
- _id: 2599F062-B435-11E9-9278-68D0E5697425
grant_number: RGY0083/2016
name: Reconstitution of cell polarity and axis determination in a cell-free system
publication: PNAS
publication_identifier:
eissn:
- '10916490'
issn:
- '00278424'
publication_status: published
publisher: National Academy of Sciences
quality_controlled: '1'
scopus_import: '1'
status: public
title: In vitro reconstitution reveals phosphoinositides as cargo-release factors
and activators of the ARF6 GAP ADAP1
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 118
year: '2021'
...
---
_id: '9243'
abstract:
- lang: eng
text: Peptidoglycan is an essential component of the bacterial cell envelope that
surrounds the cytoplasmic membrane to protect the cell from osmotic lysis. Important
antibiotics such as β-lactams and glycopeptides target peptidoglycan biosynthesis.
Class A penicillin-binding proteins (PBPs) are bifunctional membrane-bound peptidoglycan
synthases that polymerize glycan chains and connect adjacent stem peptides by
transpeptidation. How these enzymes work in their physiological membrane environment
is poorly understood. Here, we developed a novel Förster resonance energy transfer-based
assay to follow in real time both reactions of class A PBPs reconstituted in liposomes
or supported lipid bilayers and applied this assay with PBP1B homologues from
Escherichia coli, Pseudomonas aeruginosa, and Acinetobacter baumannii in the presence
or absence of their cognate lipoprotein activator. Our assay will allow unravelling
the mechanisms of peptidoglycan synthesis in a lipid-bilayer environment and can
be further developed to be used for high-throughput screening for new antimicrobials.
acknowledgement: 'We thank Alexander Egan (Newcastle University) for purified proteins
LpoB(sol) and LpoPPa(sol), Federico Corona (Newcastle University) for purified MepM,
and Oliver Birkholz and Jacob Piehler (Department of Biology and Center of Cellular
Nanoanalytics, University of Osnabru¨ ck) for their help with PBP1B reconstitution
into polymer-SLBs and initial guidance on single particle tracking. We also acknowledge
Christian P Richter and Changjiang You (Department of Biology and Center of Cellular
Nanoanalytics, University of Osnabru¨ ck) for providing SLIMfast software and tris-DODA-NTA
reagent, respectively. This work was funded by the BBSRC grant BB/R017409/1 (to
WV), the European Research Council through grant ERC-2015-StG-679239 (to ML), and
long-term fellowships HFSP LT 000824/2016-L4 and EMBO ALTF 1163–2015 (to NB). '
article_number: 1-32
article_processing_charge: No
article_type: original
author:
- first_name: Víctor M.
full_name: Hernández-Rocamora, Víctor M.
last_name: Hernández-Rocamora
- first_name: Natalia S.
full_name: Baranova, Natalia S.
id: 38661662-F248-11E8-B48F-1D18A9856A87
last_name: Baranova
orcid: 0000-0002-3086-9124
- first_name: Katharina
full_name: Peters, Katharina
last_name: Peters
- first_name: Eefjan
full_name: Breukink, Eefjan
last_name: Breukink
- first_name: Martin
full_name: Loose, Martin
id: 462D4284-F248-11E8-B48F-1D18A9856A87
last_name: Loose
orcid: 0000-0001-7309-9724
- first_name: Waldemar
full_name: Vollmer, Waldemar
last_name: Vollmer
citation:
ama: Hernández-Rocamora VM, Baranova NS, Peters K, Breukink E, Loose M, Vollmer
W. Real time monitoring of peptidoglycan synthesis by membrane-reconstituted penicillin
binding proteins. eLife. 2021;10. doi:10.7554/eLife.61525
apa: Hernández-Rocamora, V. M., Baranova, N. S., Peters, K., Breukink, E., Loose,
M., & Vollmer, W. (2021). Real time monitoring of peptidoglycan synthesis
by membrane-reconstituted penicillin binding proteins. ELife. eLife Sciences
Publications. https://doi.org/10.7554/eLife.61525
chicago: Hernández-Rocamora, Víctor M., Natalia S. Baranova, Katharina Peters, Eefjan
Breukink, Martin Loose, and Waldemar Vollmer. “Real Time Monitoring of Peptidoglycan
Synthesis by Membrane-Reconstituted Penicillin Binding Proteins.” ELife.
eLife Sciences Publications, 2021. https://doi.org/10.7554/eLife.61525.
ieee: V. M. Hernández-Rocamora, N. S. Baranova, K. Peters, E. Breukink, M. Loose,
and W. Vollmer, “Real time monitoring of peptidoglycan synthesis by membrane-reconstituted
penicillin binding proteins,” eLife, vol. 10. eLife Sciences Publications,
2021.
ista: Hernández-Rocamora VM, Baranova NS, Peters K, Breukink E, Loose M, Vollmer
W. 2021. Real time monitoring of peptidoglycan synthesis by membrane-reconstituted
penicillin binding proteins. eLife. 10, 1–32.
mla: Hernández-Rocamora, Víctor M., et al. “Real Time Monitoring of Peptidoglycan
Synthesis by Membrane-Reconstituted Penicillin Binding Proteins.” ELife,
vol. 10, 1–32, eLife Sciences Publications, 2021, doi:10.7554/eLife.61525.
short: V.M. Hernández-Rocamora, N.S. Baranova, K. Peters, E. Breukink, M. Loose,
W. Vollmer, ELife 10 (2021).
date_created: 2021-03-14T23:01:33Z
date_published: 2021-02-24T00:00:00Z
date_updated: 2023-08-07T14:10:50Z
day: '24'
ddc:
- '570'
department:
- _id: MaLo
doi: 10.7554/eLife.61525
ec_funded: 1
external_id:
isi:
- '000627596400001'
file:
- access_level: open_access
checksum: 79897a09bfecd9914d39c4aea2841855
content_type: application/pdf
creator: dernst
date_created: 2021-03-22T07:36:08Z
date_updated: 2021-03-22T07:36:08Z
file_id: '9268'
file_name: 2021_eLife_HernandezRocamora.pdf
file_size: 2314698
relation: main_file
success: 1
file_date_updated: 2021-03-22T07:36:08Z
has_accepted_license: '1'
intvolume: ' 10'
isi: 1
language:
- iso: eng
month: '02'
oa: 1
oa_version: Published Version
project:
- _id: 2595697A-B435-11E9-9278-68D0E5697425
call_identifier: H2020
grant_number: '679239'
name: Self-Organization of the Bacterial Cell
- _id: 2596EAB6-B435-11E9-9278-68D0E5697425
grant_number: ALTF 2015-1163
name: Synthesis of bacterial cell wall
- _id: 259B655A-B435-11E9-9278-68D0E5697425
grant_number: LT000824/2016
name: Reconstitution of bacterial cell wall sythesis
publication: eLife
publication_identifier:
eissn:
- 2050-084X
publication_status: published
publisher: eLife Sciences Publications
quality_controlled: '1'
scopus_import: '1'
status: public
title: Real time monitoring of peptidoglycan synthesis by membrane-reconstituted penicillin
binding proteins
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 10
year: '2021'
...
---
_id: '9414'
abstract:
- lang: eng
text: Microtubule plus-end depolymerization rate is a potentially important target
of physiological regulation, but it has been challenging to measure, so its role
in spatial organization is poorly understood. Here we apply a method for tracking
plus ends based on time difference imaging to measure depolymerization rates in
large interphase asters growing in Xenopus egg extract. We observed strong spatial
regulation of depolymerization rates, which were higher in the aster interior
compared with the periphery, and much less regulation of polymerization or catastrophe
rates. We interpret these data in terms of a limiting component model, where aster
growth results in lower levels of soluble tubulin and microtubule-associated proteins
(MAPs) in the interior cytosol compared with that at the periphery. The steady-state
polymer fraction of tubulin was ∼30%, so tubulin is not strongly depleted in the
aster interior. We propose that the limiting component for microtubule assembly
is a MAP that inhibits depolymerization, and that egg asters are tuned to low
microtubule density.
acknowledgement: The authors thank the members of Mitchison, Brugués, and Jay Gatlin
groups (University of Wyoming) for discussions. We thank Heino Andreas (MPI-CBG)
for frog maintenance. We thank Nikon for microscopy support at Marine Biological
Laboratory (MBL). K.I. was supported by fellowships from the Honjo International
Scholarship Foundation and Center of Systems Biology Dresden. F.D. was supported
by the DIGGS-BB fellowship provided by the German Research Foundation (DFG). P.C.
is supported by a Boehringer Ingelheim Fonds PhD fellowship. J.F.P. was supported
by a fellowship from the Fannie and John Hertz Foundation. M.L.’s research is supported
by European Research Council (ERC) Grant no. ERC-2015-StG-679239. J.B.’s research
is supported by the Human Frontiers Science Program (CDA00074/2014). T.J.M.’s research
is supported by National Institutes of Health Grant no. R35GM131753.
article_processing_charge: No
article_type: original
author:
- first_name: Keisuke
full_name: Ishihara, Keisuke
last_name: Ishihara
- first_name: Franziska
full_name: Decker, Franziska
last_name: Decker
- first_name: Paulo R
full_name: Dos Santos Caldas, Paulo R
id: 38FCDB4C-F248-11E8-B48F-1D18A9856A87
last_name: Dos Santos Caldas
orcid: 0000-0001-6730-4461
- first_name: James F.
full_name: Pelletier, James F.
last_name: Pelletier
- first_name: Martin
full_name: Loose, Martin
id: 462D4284-F248-11E8-B48F-1D18A9856A87
last_name: Loose
orcid: 0000-0001-7309-9724
- first_name: Jan
full_name: Brugués, Jan
last_name: Brugués
- first_name: Timothy J.
full_name: Mitchison, Timothy J.
last_name: Mitchison
citation:
ama: Ishihara K, Decker F, Dos Santos Caldas PR, et al. Spatial variation of microtubule
depolymerization in large asters. Molecular Biology of the Cell. 2021;32(9):869-879.
doi:10.1091/MBC.E20-11-0723
apa: Ishihara, K., Decker, F., Dos Santos Caldas, P. R., Pelletier, J. F., Loose,
M., Brugués, J., & Mitchison, T. J. (2021). Spatial variation of microtubule
depolymerization in large asters. Molecular Biology of the Cell. American
Society for Cell Biology. https://doi.org/10.1091/MBC.E20-11-0723
chicago: Ishihara, Keisuke, Franziska Decker, Paulo R Dos Santos Caldas, James F.
Pelletier, Martin Loose, Jan Brugués, and Timothy J. Mitchison. “Spatial Variation
of Microtubule Depolymerization in Large Asters.” Molecular Biology of the
Cell. American Society for Cell Biology, 2021. https://doi.org/10.1091/MBC.E20-11-0723.
ieee: K. Ishihara et al., “Spatial variation of microtubule depolymerization
in large asters,” Molecular Biology of the Cell, vol. 32, no. 9. American
Society for Cell Biology, pp. 869–879, 2021.
ista: Ishihara K, Decker F, Dos Santos Caldas PR, Pelletier JF, Loose M, Brugués
J, Mitchison TJ. 2021. Spatial variation of microtubule depolymerization in large
asters. Molecular Biology of the Cell. 32(9), 869–879.
mla: Ishihara, Keisuke, et al. “Spatial Variation of Microtubule Depolymerization
in Large Asters.” Molecular Biology of the Cell, vol. 32, no. 9, American
Society for Cell Biology, 2021, pp. 869–79, doi:10.1091/MBC.E20-11-0723.
short: K. Ishihara, F. Decker, P.R. Dos Santos Caldas, J.F. Pelletier, M. Loose,
J. Brugués, T.J. Mitchison, Molecular Biology of the Cell 32 (2021) 869–879.
date_created: 2021-05-23T22:01:45Z
date_published: 2021-04-19T00:00:00Z
date_updated: 2023-08-08T13:36:02Z
day: '19'
department:
- _id: MaLo
doi: 10.1091/MBC.E20-11-0723
ec_funded: 1
external_id:
isi:
- '000641574700005'
intvolume: ' 32'
isi: 1
issue: '9'
language:
- iso: eng
license: https://creativecommons.org/licenses/by-nc-sa/3.0/
main_file_link:
- open_access: '1'
url: https://www.molbiolcell.org/doi/10.1091/mbc.E20-11-0723
month: '04'
oa: 1
oa_version: Published Version
page: 869-879
project:
- _id: 2595697A-B435-11E9-9278-68D0E5697425
call_identifier: H2020
grant_number: '679239'
name: Self-Organization of the Bacterial Cell
- _id: 260D98C8-B435-11E9-9278-68D0E5697425
name: Reconstitution of Bacterial Cell Division Using Purified Components
publication: Molecular Biology of the Cell
publication_identifier:
eissn:
- 1939-4586
issn:
- 1059-1524
publication_status: published
publisher: American Society for Cell Biology
quality_controlled: '1'
scopus_import: '1'
status: public
title: Spatial variation of microtubule depolymerization in large asters
tmp:
image: /images/cc_by_nc_sa.png
legal_code_url: https://creativecommons.org/licenses/by-nc-sa/3.0/legalcode
name: Creative Commons Attribution-NonCommercial-ShareAlike 3.0 Unported (CC BY-NC-SA
3.0)
short: CC BY-NC-SA (3.0)
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 32
year: '2021'
...
---
_id: '9887'
abstract:
- lang: eng
text: Clathrin-mediated endocytosis is the major route of entry of cargos into cells
and thus underpins many physiological processes. During endocytosis, an area of
flat membrane is remodeled by proteins to create a spherical vesicle against intracellular
forces. The protein machinery which mediates this membrane bending in plants is
unknown. However, it is known that plant endocytosis is actin independent, thus
indicating that plants utilize a unique mechanism to mediate membrane bending
against high-turgor pressure compared to other model systems. Here, we investigate
the TPLATE complex, a plant-specific endocytosis protein complex. It has been
thought to function as a classical adaptor functioning underneath the clathrin
coat. However, by using biochemical and advanced live microscopy approaches, we
found that TPLATE is peripherally associated with clathrin-coated vesicles and
localizes at the rim of endocytosis events. As this localization is more fitting
to the protein machinery involved in membrane bending during endocytosis, we examined
cells in which the TPLATE complex was disrupted and found that the clathrin structures
present as flat patches. This suggests a requirement of the TPLATE complex for
membrane bending during plant clathrin–mediated endocytosis. Next, we used in
vitro biophysical assays to confirm that the TPLATE complex possesses protein
domains with intrinsic membrane remodeling activity. These results redefine the
role of the TPLATE complex and implicate it as a key component of the evolutionarily
distinct plant endocytosis mechanism, which mediates endocytic membrane bending
against the high-turgor pressure in plant cells.
acknowledged_ssus:
- _id: EM-Fac
- _id: LifeSc
- _id: Bio
acknowledgement: 'We gratefully thank Julie Neveu and Dr. Amanda Barranco of the Grégory
Vert laboratory for help preparing plants in France, Dr. Zuzana Gelova for help
and advice with protoplast generation, Dr. Stéphane Vassilopoulos and Dr. Florian
Schur for advice regarding EM tomography, Alejandro Marquiegui Alvaro for help with
material generation, and Dr. Lukasz Kowalski for generously gifting us the mWasabi
protein. This research was supported by the Scientific Service Units of Institute
of Science and Technology Austria (IST Austria) through resources provided by the
Electron Microscopy Facility, Lab Support Facility (particularly Dorota Jaworska),
and the Bioimaging Facility. We acknowledge the Advanced Microscopy Facility of
the Vienna BioCenter Core Facilities for use of the 3D SIM. For the mass spectrometry
analysis of proteins, we acknowledge the University of Natural Resources and Life
Sciences (BOKU) Core Facility Mass Spectrometry. This work was supported by the
following funds: A.J. is supported by funding from the Austrian Science Fund I3630B25
to J.F. P.M. and E.B. are supported by Agence Nationale de la Recherche ANR-11-EQPX-0029
Morphoscope2 and ANR-10-INBS-04 France BioImaging. S.Y.B. is supported by the NSF
No. 1121998 and 1614915. J.W. and D.V.D. are supported by the European Research
Council Grant 682436 (to D.V.D.), a China Scholarship Council Grant 201508440249
(to J.W.), and by a Ghent University Special Research Co-funding Grant ST01511051
(to J.W.).'
article_number: e2113046118
article_processing_charge: No
article_type: original
author:
- first_name: Alexander J
full_name: Johnson, Alexander J
id: 46A62C3A-F248-11E8-B48F-1D18A9856A87
last_name: Johnson
orcid: 0000-0002-2739-8843
- first_name: Dana A
full_name: Dahhan, Dana A
last_name: Dahhan
- first_name: Nataliia
full_name: Gnyliukh, Nataliia
id: 390C1120-F248-11E8-B48F-1D18A9856A87
last_name: Gnyliukh
orcid: 0000-0002-2198-0509
- first_name: Walter
full_name: Kaufmann, Walter
id: 3F99E422-F248-11E8-B48F-1D18A9856A87
last_name: Kaufmann
orcid: 0000-0001-9735-5315
- first_name: Vanessa
full_name: Zheden, Vanessa
id: 39C5A68A-F248-11E8-B48F-1D18A9856A87
last_name: Zheden
orcid: 0000-0002-9438-4783
- first_name: Tommaso
full_name: Costanzo, Tommaso
id: D93824F4-D9BA-11E9-BB12-F207E6697425
last_name: Costanzo
orcid: 0000-0001-9732-3815
- first_name: Pierre
full_name: Mahou, Pierre
last_name: Mahou
- first_name: Mónika
full_name: Hrtyan, Mónika
id: 45A71A74-F248-11E8-B48F-1D18A9856A87
last_name: Hrtyan
- first_name: Jie
full_name: Wang, Jie
last_name: Wang
- first_name: Juan L
full_name: Aguilera Servin, Juan L
id: 2A67C376-F248-11E8-B48F-1D18A9856A87
last_name: Aguilera Servin
orcid: 0000-0002-2862-8372
- first_name: Daniël
full_name: van Damme, Daniël
last_name: van Damme
- first_name: Emmanuel
full_name: Beaurepaire, Emmanuel
last_name: Beaurepaire
- first_name: Martin
full_name: Loose, Martin
id: 462D4284-F248-11E8-B48F-1D18A9856A87
last_name: Loose
orcid: 0000-0001-7309-9724
- first_name: Sebastian Y
full_name: Bednarek, Sebastian Y
last_name: Bednarek
- first_name: Jiří
full_name: Friml, Jiří
id: 4159519E-F248-11E8-B48F-1D18A9856A87
last_name: Friml
orcid: 0000-0002-8302-7596
citation:
ama: Johnson AJ, Dahhan DA, Gnyliukh N, et al. The TPLATE complex mediates membrane
bending during plant clathrin-mediated endocytosis. Proceedings of the National
Academy of Sciences. 2021;118(51). doi:10.1073/pnas.2113046118
apa: Johnson, A. J., Dahhan, D. A., Gnyliukh, N., Kaufmann, W., Zheden, V., Costanzo,
T., … Friml, J. (2021). The TPLATE complex mediates membrane bending during plant
clathrin-mediated endocytosis. Proceedings of the National Academy of Sciences.
National Academy of Sciences. https://doi.org/10.1073/pnas.2113046118
chicago: Johnson, Alexander J, Dana A Dahhan, Nataliia Gnyliukh, Walter Kaufmann,
Vanessa Zheden, Tommaso Costanzo, Pierre Mahou, et al. “The TPLATE Complex Mediates
Membrane Bending during Plant Clathrin-Mediated Endocytosis.” Proceedings of
the National Academy of Sciences. National Academy of Sciences, 2021. https://doi.org/10.1073/pnas.2113046118.
ieee: A. J. Johnson et al., “The TPLATE complex mediates membrane bending
during plant clathrin-mediated endocytosis,” Proceedings of the National Academy
of Sciences, vol. 118, no. 51. National Academy of Sciences, 2021.
ista: Johnson AJ, Dahhan DA, Gnyliukh N, Kaufmann W, Zheden V, Costanzo T, Mahou
P, Hrtyan M, Wang J, Aguilera Servin JL, van Damme D, Beaurepaire E, Loose M,
Bednarek SY, Friml J. 2021. The TPLATE complex mediates membrane bending during
plant clathrin-mediated endocytosis. Proceedings of the National Academy of Sciences.
118(51), e2113046118.
mla: Johnson, Alexander J., et al. “The TPLATE Complex Mediates Membrane Bending
during Plant Clathrin-Mediated Endocytosis.” Proceedings of the National Academy
of Sciences, vol. 118, no. 51, e2113046118, National Academy of Sciences,
2021, doi:10.1073/pnas.2113046118.
short: A.J. Johnson, D.A. Dahhan, N. Gnyliukh, W. Kaufmann, V. Zheden, T. Costanzo,
P. Mahou, M. Hrtyan, J. Wang, J.L. Aguilera Servin, D. van Damme, E. Beaurepaire,
M. Loose, S.Y. Bednarek, J. Friml, Proceedings of the National Academy of Sciences
118 (2021).
date_created: 2021-08-11T14:11:43Z
date_published: 2021-12-14T00:00:00Z
date_updated: 2024-02-19T11:06:09Z
day: '14'
ddc:
- '580'
department:
- _id: JiFr
- _id: MaLo
- _id: EvBe
- _id: EM-Fac
- _id: NanoFab
doi: 10.1073/pnas.2113046118
external_id:
isi:
- '000736417600043'
pmid:
- '34907016'
file:
- access_level: open_access
checksum: 8d01e72e22c4fb1584e72d8601947069
content_type: application/pdf
creator: cchlebak
date_created: 2021-12-15T08:59:40Z
date_updated: 2021-12-15T08:59:40Z
file_id: '10546'
file_name: 2021_PNAS_Johnson.pdf
file_size: 2757340
relation: main_file
success: 1
file_date_updated: 2021-12-15T08:59:40Z
has_accepted_license: '1'
intvolume: ' 118'
isi: 1
issue: '51'
language:
- iso: eng
month: '12'
oa: 1
oa_version: Published Version
pmid: 1
project:
- _id: 26538374-B435-11E9-9278-68D0E5697425
call_identifier: FWF
grant_number: I03630
name: Molecular mechanisms of endocytic cargo recognition in plants
publication: Proceedings of the National Academy of Sciences
publication_identifier:
eissn:
- 1091-6490
publication_status: published
publisher: National Academy of Sciences
quality_controlled: '1'
related_material:
link:
- relation: earlier_version
url: https://doi.org/10.1101/2021.04.26.441441
record:
- id: '14510'
relation: dissertation_contains
status: public
- id: '14988'
relation: research_data
status: public
status: public
title: The TPLATE complex mediates membrane bending during plant clathrin-mediated
endocytosis
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 118
year: '2021'
...
---
_id: '9907'
abstract:
- lang: eng
text: 'DivIVA is a protein initially identified as a spatial regulator of cell division
in the model organism Bacillus subtilis, but its homologues are present in many
other Gram-positive bacteria, including Clostridia species. Besides its role as
topological regulator of the Min system during bacterial cell division, DivIVA
is involved in chromosome segregation during sporulation, genetic competence,
and cell wall synthesis. DivIVA localizes to regions of high membrane curvature,
such as the cell poles and cell division site, where it recruits distinct binding
partners. Previously, it was suggested that negative curvature sensing is the
main mechanism by which DivIVA binds to these specific regions. Here, we show
that Clostridioides difficile DivIVA binds preferably to membranes containing
negatively charged phospholipids, especially cardiolipin. Strikingly, we observed
that upon binding, DivIVA modifies the lipid distribution and induces changes
to lipid bilayers containing cardiolipin. Our observations indicate that DivIVA
might play a more complex and so far unknown active role during the formation
of the cell division septal membrane. '
acknowledged_ssus:
- _id: Bio
- _id: LifeSc
acknowledgement: "We thank Daniela Krajˇcíkova, Katarína Muchová, Zuzana Chromíkova
and other members of Barák’s laboratory for useful discussions, suggestions and
help. Special thanks also to Emília Chovancová for technical support. We are grateful
to Juraj Labaj for drawing the model and for help with graphics. Many thanks to
all members of Loose’s laboratory: Maria del Mar\r\nLópez, Paulo Caldas, Philipp
Radler, and other members of the Loose’s laboratory for sharing their knowledge
of SLB preparation and TIRF experiment chambers, for sharing coverslips and for
help with the TIRF microscope and data analysis. We also thank the members of the
Dept. of Biochemistry of Biomembranes at the Institute of Animal Biochemistry and
Genetics, CBs SAS for their help with preparing the lipid mixtures. We thank J.
Bauer for critically reading the manuscript."
article_number: '8350'
article_processing_charge: Yes
article_type: original
author:
- first_name: Naďa
full_name: Labajová, Naďa
last_name: Labajová
- first_name: Natalia S.
full_name: Baranova, Natalia S.
id: 38661662-F248-11E8-B48F-1D18A9856A87
last_name: Baranova
orcid: 0000-0002-3086-9124
- first_name: Miroslav
full_name: Jurásek, Miroslav
last_name: Jurásek
- first_name: Robert
full_name: Vácha, Robert
last_name: Vácha
- first_name: Martin
full_name: Loose, Martin
id: 462D4284-F248-11E8-B48F-1D18A9856A87
last_name: Loose
orcid: 0000-0001-7309-9724
- first_name: Imrich
full_name: Barák, Imrich
last_name: Barák
citation:
ama: Labajová N, Baranova NS, Jurásek M, Vácha R, Loose M, Barák I. Cardiolipin-containing
lipid membranes attract the bacterial cell division protein diviva. International
Journal of Molecular Sciences. 2021;22(15). doi:10.3390/ijms22158350
apa: Labajová, N., Baranova, N. S., Jurásek, M., Vácha, R., Loose, M., & Barák,
I. (2021). Cardiolipin-containing lipid membranes attract the bacterial cell division
protein diviva. International Journal of Molecular Sciences. MDPI. https://doi.org/10.3390/ijms22158350
chicago: Labajová, Naďa, Natalia S. Baranova, Miroslav Jurásek, Robert Vácha, Martin
Loose, and Imrich Barák. “Cardiolipin-Containing Lipid Membranes Attract the Bacterial
Cell Division Protein Diviva.” International Journal of Molecular Sciences.
MDPI, 2021. https://doi.org/10.3390/ijms22158350.
ieee: N. Labajová, N. S. Baranova, M. Jurásek, R. Vácha, M. Loose, and I. Barák,
“Cardiolipin-containing lipid membranes attract the bacterial cell division protein
diviva,” International Journal of Molecular Sciences, vol. 22, no. 15.
MDPI, 2021.
ista: Labajová N, Baranova NS, Jurásek M, Vácha R, Loose M, Barák I. 2021. Cardiolipin-containing
lipid membranes attract the bacterial cell division protein diviva. International
Journal of Molecular Sciences. 22(15), 8350.
mla: Labajová, Naďa, et al. “Cardiolipin-Containing Lipid Membranes Attract the
Bacterial Cell Division Protein Diviva.” International Journal of Molecular
Sciences, vol. 22, no. 15, 8350, MDPI, 2021, doi:10.3390/ijms22158350.
short: N. Labajová, N.S. Baranova, M. Jurásek, R. Vácha, M. Loose, I. Barák, International
Journal of Molecular Sciences 22 (2021).
date_created: 2021-08-15T22:01:27Z
date_published: 2021-08-01T00:00:00Z
date_updated: 2023-08-11T10:34:44Z
day: '01'
ddc:
- '570'
department:
- _id: MaLo
doi: 10.3390/ijms22158350
ec_funded: 1
external_id:
isi:
- '000681815400001'
pmid:
- '34361115'
file:
- access_level: open_access
checksum: a4bc06e9a2c803ceff5a91f10b174054
content_type: application/pdf
creator: asandaue
date_created: 2021-08-16T09:35:56Z
date_updated: 2021-08-16T09:35:56Z
file_id: '9923'
file_name: 2021_InternationalJournalOfMolecularSciences_Labajová .pdf
file_size: 6132410
relation: main_file
success: 1
file_date_updated: 2021-08-16T09:35:56Z
has_accepted_license: '1'
intvolume: ' 22'
isi: 1
issue: '15'
language:
- iso: eng
month: '08'
oa: 1
oa_version: Published Version
pmid: 1
project:
- _id: 2595697A-B435-11E9-9278-68D0E5697425
call_identifier: H2020
grant_number: '679239'
name: Self-Organization of the Bacterial Cell
publication: International Journal of Molecular Sciences
publication_identifier:
eissn:
- '14220067'
issn:
- '16616596'
publication_status: published
publisher: MDPI
quality_controlled: '1'
scopus_import: '1'
status: public
title: Cardiolipin-containing lipid membranes attract the bacterial cell division
protein diviva
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 22
year: '2021'
...
---
_id: '7387'
abstract:
- lang: eng
text: Most bacteria accomplish cell division with the help of a dynamic protein
complex called the divisome, which spans the cell envelope in the plane of division.
Assembly and activation of this machinery are coordinated by the tubulin-related
GTPase FtsZ, which was found to form treadmilling filaments on supported bilayers
in vitro1, as well as in live cells, in which filaments circle around the cell
division site2,3. Treadmilling of FtsZ is thought to actively move proteins around
the division septum, thereby distributing peptidoglycan synthesis and coordinating
the inward growth of the septum to form the new poles of the daughter cells4.
However, the molecular mechanisms underlying this function are largely unknown.
Here, to study how FtsZ polymerization dynamics are coupled to downstream proteins,
we reconstituted part of the bacterial cell division machinery using its purified
components FtsZ, FtsA and truncated transmembrane proteins essential for cell
division. We found that the membrane-bound cytosolic peptides of FtsN and FtsQ
co-migrated with treadmilling FtsZ–FtsA filaments, but despite their directed
collective behaviour, individual peptides showed random motion and transient confinement.
Our work suggests that divisome proteins follow treadmilling FtsZ filaments by
a diffusion-and-capture mechanism, which can give rise to a moving zone of signalling
activity at the division site.
acknowledgement: We acknowledge members of the Loose laboratory at IST Austria for
helpful discussions—in particular, P. Caldas for help with the treadmilling analysis,
M. Jimenez, A. Raso and N. Ropero for providing Alexa Fluor 488- and Alexa Fluor
647-labelled FtsA for the MST and analytical ultracentrifugation experiments. We
thank C. You for providing the DODA-tris-NTA phospholipids, as well as J. Piehler
and C. Richter (Department of Biology, University of Osnabruck, Germany) for the
SLIMfast single-molecule tracking software and help with the confinement analysis.
We thank J. Errington and H. Murray (both at Newcastle University, UK) for critical
reading of the manuscript, and J. Brugués (MPI-CBG and MPI-PKS, Dresden, Germany)
for help with the MATLAB programming and reading of the manuscript. This work was
supported by the European Research Council through grant ERC-2015-StG-679239 to
M.L. and grants HFSP LT 000824/2016-L4 and EMBO ALTF 1163-2015 to N.B., a grant
from the Ministry of Economy and Competitiveness of the Spanish Government (BFU2016-75471-C2-1-P)
to C.A. and G.R., and a Wellcome Trust Senior Investigator award (101824/Z/13/Z)
and a grant from the BBSRC (BB/R017409/1) to W.V.
article_processing_charge: No
article_type: letter_note
author:
- first_name: Natalia S.
full_name: Baranova, Natalia S.
id: 38661662-F248-11E8-B48F-1D18A9856A87
last_name: Baranova
orcid: 0000-0002-3086-9124
- first_name: Philipp
full_name: Radler, Philipp
id: 40136C2A-F248-11E8-B48F-1D18A9856A87
last_name: Radler
orcid: '0000-0001-9198-2182 '
- first_name: Víctor M.
full_name: Hernández-Rocamora, Víctor M.
last_name: Hernández-Rocamora
- first_name: Carlos
full_name: Alfonso, Carlos
last_name: Alfonso
- first_name: Maria D
full_name: Lopez Pelegrin, Maria D
id: 319AA9CE-F248-11E8-B48F-1D18A9856A87
last_name: Lopez Pelegrin
- first_name: Germán
full_name: Rivas, Germán
last_name: Rivas
- first_name: Waldemar
full_name: Vollmer, Waldemar
last_name: Vollmer
- first_name: Martin
full_name: Loose, Martin
id: 462D4284-F248-11E8-B48F-1D18A9856A87
last_name: Loose
orcid: 0000-0001-7309-9724
citation:
ama: Baranova NS, Radler P, Hernández-Rocamora VM, et al. Diffusion and capture
permits dynamic coupling between treadmilling FtsZ filaments and cell division
proteins. Nature Microbiology. 2020;5:407-417. doi:10.1038/s41564-019-0657-5
apa: Baranova, N. S., Radler, P., Hernández-Rocamora, V. M., Alfonso, C., Lopez
Pelegrin, M. D., Rivas, G., … Loose, M. (2020). Diffusion and capture permits
dynamic coupling between treadmilling FtsZ filaments and cell division proteins.
Nature Microbiology. Springer Nature. https://doi.org/10.1038/s41564-019-0657-5
chicago: Baranova, Natalia S., Philipp Radler, Víctor M. Hernández-Rocamora, Carlos
Alfonso, Maria D Lopez Pelegrin, Germán Rivas, Waldemar Vollmer, and Martin Loose.
“Diffusion and Capture Permits Dynamic Coupling between Treadmilling FtsZ Filaments
and Cell Division Proteins.” Nature Microbiology. Springer Nature, 2020.
https://doi.org/10.1038/s41564-019-0657-5.
ieee: N. S. Baranova et al., “Diffusion and capture permits dynamic coupling
between treadmilling FtsZ filaments and cell division proteins,” Nature Microbiology,
vol. 5. Springer Nature, pp. 407–417, 2020.
ista: Baranova NS, Radler P, Hernández-Rocamora VM, Alfonso C, Lopez Pelegrin MD,
Rivas G, Vollmer W, Loose M. 2020. Diffusion and capture permits dynamic coupling
between treadmilling FtsZ filaments and cell division proteins. Nature Microbiology.
5, 407–417.
mla: Baranova, Natalia S., et al. “Diffusion and Capture Permits Dynamic Coupling
between Treadmilling FtsZ Filaments and Cell Division Proteins.” Nature Microbiology,
vol. 5, Springer Nature, 2020, pp. 407–17, doi:10.1038/s41564-019-0657-5.
short: N.S. Baranova, P. Radler, V.M. Hernández-Rocamora, C. Alfonso, M.D. Lopez
Pelegrin, G. Rivas, W. Vollmer, M. Loose, Nature Microbiology 5 (2020) 407–417.
date_created: 2020-01-28T16:14:41Z
date_published: 2020-01-20T00:00:00Z
date_updated: 2023-10-06T12:22:38Z
day: '20'
department:
- _id: MaLo
doi: 10.1038/s41564-019-0657-5
ec_funded: 1
external_id:
isi:
- '000508584700007'
pmid:
- '31959972'
intvolume: ' 5'
isi: 1
language:
- iso: eng
main_file_link:
- open_access: '1'
url: http://europepmc.org/article/PMC/7048620
month: '01'
oa: 1
oa_version: Submitted Version
page: 407-417
pmid: 1
project:
- _id: 2595697A-B435-11E9-9278-68D0E5697425
call_identifier: H2020
grant_number: '679239'
name: Self-Organization of the Bacterial Cell
- _id: 259B655A-B435-11E9-9278-68D0E5697425
grant_number: LT000824/2016
name: Reconstitution of bacterial cell wall sythesis
- _id: 2596EAB6-B435-11E9-9278-68D0E5697425
grant_number: ALTF 2015-1163
name: Synthesis of bacterial cell wall
publication: Nature Microbiology
publication_identifier:
issn:
- 2058-5276
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
related_material:
link:
- description: News on IST Homepage
relation: press_release
url: https://ist.ac.at/en/news/little-cell-big-cover-story/
record:
- id: '14280'
relation: dissertation_contains
status: public
scopus_import: '1'
status: public
title: Diffusion and capture permits dynamic coupling between treadmilling FtsZ filaments
and cell division proteins
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 5
year: '2020'
...
---
_id: '7572'
abstract:
- lang: eng
text: The polymerization–depolymerization dynamics of cytoskeletal proteins play
essential roles in the self-organization of cytoskeletal structures, in eukaryotic
as well as prokaryotic cells. While advances in fluorescence microscopy and in
vitro reconstitution experiments have helped to study the dynamic properties of
these complex systems, methods that allow to collect and analyze large quantitative
datasets of the underlying polymer dynamics are still missing. Here, we present
a novel image analysis workflow to study polymerization dynamics of active filaments
in a nonbiased, highly automated manner. Using treadmilling filaments of the bacterial
tubulin FtsZ as an example, we demonstrate that our method is able to specifically
detect, track and analyze growth and shrinkage of polymers, even in dense networks
of filaments. We believe that this automated method can facilitate the analysis
of a large variety of dynamic cytoskeletal systems, using standard time-lapse
movies obtained from experiments in vitro as well as in the living cell. Moreover,
we provide scripts implementing this method as supplementary material.
alternative_title:
- Methods in Cell Biology
article_processing_charge: No
author:
- first_name: Paulo R
full_name: Dos Santos Caldas, Paulo R
id: 38FCDB4C-F248-11E8-B48F-1D18A9856A87
last_name: Dos Santos Caldas
orcid: 0000-0001-6730-4461
- first_name: Philipp
full_name: Radler, Philipp
id: 40136C2A-F248-11E8-B48F-1D18A9856A87
last_name: Radler
orcid: '0000-0001-9198-2182 '
- first_name: Christoph M
full_name: Sommer, Christoph M
id: 4DF26D8C-F248-11E8-B48F-1D18A9856A87
last_name: Sommer
orcid: 0000-0003-1216-9105
- first_name: Martin
full_name: Loose, Martin
id: 462D4284-F248-11E8-B48F-1D18A9856A87
last_name: Loose
orcid: 0000-0001-7309-9724
citation:
ama: 'Dos Santos Caldas PR, Radler P, Sommer CM, Loose M. Computational analysis
of filament polymerization dynamics in cytoskeletal networks. In: Tran P, ed.
Methods in Cell Biology. Vol 158. Elsevier; 2020:145-161. doi:10.1016/bs.mcb.2020.01.006'
apa: Dos Santos Caldas, P. R., Radler, P., Sommer, C. M., & Loose, M. (2020).
Computational analysis of filament polymerization dynamics in cytoskeletal networks.
In P. Tran (Ed.), Methods in Cell Biology (Vol. 158, pp. 145–161). Elsevier.
https://doi.org/10.1016/bs.mcb.2020.01.006
chicago: Dos Santos Caldas, Paulo R, Philipp Radler, Christoph M Sommer, and Martin
Loose. “Computational Analysis of Filament Polymerization Dynamics in Cytoskeletal
Networks.” In Methods in Cell Biology, edited by Phong Tran, 158:145–61.
Elsevier, 2020. https://doi.org/10.1016/bs.mcb.2020.01.006.
ieee: P. R. Dos Santos Caldas, P. Radler, C. M. Sommer, and M. Loose, “Computational
analysis of filament polymerization dynamics in cytoskeletal networks,” in Methods
in Cell Biology, vol. 158, P. Tran, Ed. Elsevier, 2020, pp. 145–161.
ista: 'Dos Santos Caldas PR, Radler P, Sommer CM, Loose M. 2020.Computational analysis
of filament polymerization dynamics in cytoskeletal networks. In: Methods in Cell
Biology. Methods in Cell Biology, vol. 158, 145–161.'
mla: Dos Santos Caldas, Paulo R., et al. “Computational Analysis of Filament Polymerization
Dynamics in Cytoskeletal Networks.” Methods in Cell Biology, edited by
Phong Tran, vol. 158, Elsevier, 2020, pp. 145–61, doi:10.1016/bs.mcb.2020.01.006.
short: P.R. Dos Santos Caldas, P. Radler, C.M. Sommer, M. Loose, in:, P. Tran (Ed.),
Methods in Cell Biology, Elsevier, 2020, pp. 145–161.
date_created: 2020-03-08T23:00:47Z
date_published: 2020-02-27T00:00:00Z
date_updated: 2023-10-04T09:50:24Z
day: '27'
department:
- _id: MaLo
doi: 10.1016/bs.mcb.2020.01.006
ec_funded: 1
editor:
- first_name: 'Phong '
full_name: 'Tran, Phong '
last_name: Tran
external_id:
isi:
- '000611826500008'
intvolume: ' 158'
isi: 1
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1101/839571
month: '02'
oa: 1
oa_version: Preprint
page: 145-161
project:
- _id: 2595697A-B435-11E9-9278-68D0E5697425
call_identifier: H2020
grant_number: '679239'
name: Self-Organization of the Bacterial Cell
- _id: 260D98C8-B435-11E9-9278-68D0E5697425
name: Reconstitution of Bacterial Cell Division Using Purified Components
publication: Methods in Cell Biology
publication_identifier:
issn:
- 0091679X
publication_status: published
publisher: Elsevier
quality_controlled: '1'
related_material:
record:
- id: '8358'
relation: part_of_dissertation
status: public
scopus_import: '1'
status: public
title: Computational analysis of filament polymerization dynamics in cytoskeletal
networks
type: book_chapter
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 158
year: '2020'
...
---
_id: '7580'
abstract:
- lang: eng
text: The eukaryotic endomembrane system is controlled by small GTPases of the Rab
family, which are activated at defined times and locations in a switch-like manner.
While this switch is well understood for an individual protein, how regulatory
networks produce intracellular activity patterns is currently not known. Here,
we combine in vitro reconstitution experiments with computational modeling to
study a minimal Rab5 activation network. We find that the molecular interactions
in this system give rise to a positive feedback and bistable collective switching
of Rab5. Furthermore, we find that switching near the critical point is intrinsically
stochastic and provide evidence that controlling the inactive population of Rab5
on the membrane can shape the network response. Notably, we demonstrate that collective
switching can spread on the membrane surface as a traveling wave of Rab5 activation.
Together, our findings reveal how biochemical signaling networks control vesicle
trafficking pathways and how their nonequilibrium properties define the spatiotemporal
organization of the cell.
acknowledged_ssus:
- _id: Bio
- _id: LifeSc
article_processing_charge: No
article_type: original
author:
- first_name: Urban
full_name: Bezeljak, Urban
id: 2A58201A-F248-11E8-B48F-1D18A9856A87
last_name: Bezeljak
orcid: 0000-0003-1365-5631
- first_name: Hrushikesh
full_name: Loya, Hrushikesh
last_name: Loya
- first_name: Beata M
full_name: Kaczmarek, Beata M
id: 36FA4AFA-F248-11E8-B48F-1D18A9856A87
last_name: Kaczmarek
- first_name: Timothy E.
full_name: Saunders, Timothy E.
last_name: Saunders
- first_name: Martin
full_name: Loose, Martin
id: 462D4284-F248-11E8-B48F-1D18A9856A87
last_name: Loose
orcid: 0000-0001-7309-9724
citation:
ama: Bezeljak U, Loya H, Kaczmarek BM, Saunders TE, Loose M. Stochastic activation
and bistability in a Rab GTPase regulatory network. Proceedings of the National
Academy of Sciences. 2020;117(12):6504-6549. doi:10.1073/pnas.1921027117
apa: Bezeljak, U., Loya, H., Kaczmarek, B. M., Saunders, T. E., & Loose, M.
(2020). Stochastic activation and bistability in a Rab GTPase regulatory network.
Proceedings of the National Academy of Sciences. Proceedings of the National
Academy of Sciences. https://doi.org/10.1073/pnas.1921027117
chicago: Bezeljak, Urban, Hrushikesh Loya, Beata M Kaczmarek, Timothy E. Saunders,
and Martin Loose. “Stochastic Activation and Bistability in a Rab GTPase Regulatory
Network.” Proceedings of the National Academy of Sciences. Proceedings
of the National Academy of Sciences, 2020. https://doi.org/10.1073/pnas.1921027117.
ieee: U. Bezeljak, H. Loya, B. M. Kaczmarek, T. E. Saunders, and M. Loose, “Stochastic
activation and bistability in a Rab GTPase regulatory network,” Proceedings
of the National Academy of Sciences, vol. 117, no. 12. Proceedings of the
National Academy of Sciences, pp. 6504–6549, 2020.
ista: Bezeljak U, Loya H, Kaczmarek BM, Saunders TE, Loose M. 2020. Stochastic activation
and bistability in a Rab GTPase regulatory network. Proceedings of the National
Academy of Sciences. 117(12), 6504–6549.
mla: Bezeljak, Urban, et al. “Stochastic Activation and Bistability in a Rab GTPase
Regulatory Network.” Proceedings of the National Academy of Sciences, vol.
117, no. 12, Proceedings of the National Academy of Sciences, 2020, pp. 6504–49,
doi:10.1073/pnas.1921027117.
short: U. Bezeljak, H. Loya, B.M. Kaczmarek, T.E. Saunders, M. Loose, Proceedings
of the National Academy of Sciences 117 (2020) 6504–6549.
date_created: 2020-03-12T05:32:26Z
date_published: 2020-03-24T00:00:00Z
date_updated: 2023-09-07T13:17:06Z
day: '24'
department:
- _id: MaLo
- _id: CaBe
doi: 10.1073/pnas.1921027117
external_id:
isi:
- '000521821800040'
intvolume: ' 117'
isi: 1
issue: '12'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1101/776567
month: '03'
oa: 1
oa_version: Preprint
page: 6504-6549
project:
- _id: 2599F062-B435-11E9-9278-68D0E5697425
grant_number: RGY0083/2016
name: Reconstitution of cell polarity and axis determination in a cell-free system
publication: Proceedings of the National Academy of Sciences
publication_identifier:
eissn:
- 1091-6490
issn:
- 0027-8424
publication_status: published
publisher: Proceedings of the National Academy of Sciences
quality_controlled: '1'
related_material:
link:
- description: News on IST Homepage
relation: press_release
url: https://ist.ac.at/en/news/proteins-as-molecular-switches/
record:
- id: '8341'
relation: dissertation_contains
status: public
scopus_import: '1'
status: public
title: Stochastic activation and bistability in a Rab GTPase regulatory network
type: journal_article
user_id: c635000d-4b10-11ee-a964-aac5a93f6ac1
volume: 117
year: '2020'
...
---
_id: '7197'
abstract:
- lang: eng
text: During bacterial cell division, the tubulin-homolog FtsZ forms a ring-like
structure at the center of the cell. This Z-ring not only organizes the division
machinery, but treadmilling of FtsZ filaments was also found to play a key role
in distributing proteins at the division site. What regulates the architecture,
dynamics and stability of the Z-ring is currently unknown, but FtsZ-associated
proteins are known to play an important role. Here, using an in vitro reconstitution
approach, we studied how the well-conserved protein ZapA affects FtsZ treadmilling
and filament organization into large-scale patterns. Using high-resolution fluorescence
microscopy and quantitative image analysis, we found that ZapA cooperatively increases
the spatial order of the filament network, but binds only transiently to FtsZ
filaments and has no effect on filament length and treadmilling velocity. Together,
our data provides a model for how FtsZ-associated proteins can increase the precision
and stability of the bacterial cell division machinery in a switch-like manner.
acknowledged_ssus:
- _id: LifeSc
- _id: Bio
article_number: '5744'
article_processing_charge: No
article_type: original
author:
- first_name: Paulo R
full_name: Dos Santos Caldas, Paulo R
id: 38FCDB4C-F248-11E8-B48F-1D18A9856A87
last_name: Dos Santos Caldas
orcid: 0000-0001-6730-4461
- first_name: Maria D
full_name: Lopez Pelegrin, Maria D
id: 319AA9CE-F248-11E8-B48F-1D18A9856A87
last_name: Lopez Pelegrin
- first_name: Daniel J. G.
full_name: Pearce, Daniel J. G.
last_name: Pearce
- first_name: Nazmi B
full_name: Budanur, Nazmi B
id: 3EA1010E-F248-11E8-B48F-1D18A9856A87
last_name: Budanur
orcid: 0000-0003-0423-5010
- first_name: Jan
full_name: Brugués, Jan
last_name: Brugués
- first_name: Martin
full_name: Loose, Martin
id: 462D4284-F248-11E8-B48F-1D18A9856A87
last_name: Loose
orcid: 0000-0001-7309-9724
citation:
ama: Dos Santos Caldas PR, Lopez Pelegrin MD, Pearce DJG, Budanur NB, Brugués J,
Loose M. Cooperative ordering of treadmilling filaments in cytoskeletal networks
of FtsZ and its crosslinker ZapA. Nature Communications. 2019;10. doi:10.1038/s41467-019-13702-4
apa: Dos Santos Caldas, P. R., Lopez Pelegrin, M. D., Pearce, D. J. G., Budanur,
N. B., Brugués, J., & Loose, M. (2019). Cooperative ordering of treadmilling
filaments in cytoskeletal networks of FtsZ and its crosslinker ZapA. Nature
Communications. Springer Nature. https://doi.org/10.1038/s41467-019-13702-4
chicago: Dos Santos Caldas, Paulo R, Maria D Lopez Pelegrin, Daniel J. G. Pearce,
Nazmi B Budanur, Jan Brugués, and Martin Loose. “Cooperative Ordering of Treadmilling
Filaments in Cytoskeletal Networks of FtsZ and Its Crosslinker ZapA.” Nature
Communications. Springer Nature, 2019. https://doi.org/10.1038/s41467-019-13702-4.
ieee: P. R. Dos Santos Caldas, M. D. Lopez Pelegrin, D. J. G. Pearce, N. B. Budanur,
J. Brugués, and M. Loose, “Cooperative ordering of treadmilling filaments in cytoskeletal
networks of FtsZ and its crosslinker ZapA,” Nature Communications, vol.
10. Springer Nature, 2019.
ista: Dos Santos Caldas PR, Lopez Pelegrin MD, Pearce DJG, Budanur NB, Brugués J,
Loose M. 2019. Cooperative ordering of treadmilling filaments in cytoskeletal
networks of FtsZ and its crosslinker ZapA. Nature Communications. 10, 5744.
mla: Dos Santos Caldas, Paulo R., et al. “Cooperative Ordering of Treadmilling Filaments
in Cytoskeletal Networks of FtsZ and Its Crosslinker ZapA.” Nature Communications,
vol. 10, 5744, Springer Nature, 2019, doi:10.1038/s41467-019-13702-4.
short: P.R. Dos Santos Caldas, M.D. Lopez Pelegrin, D.J.G. Pearce, N.B. Budanur,
J. Brugués, M. Loose, Nature Communications 10 (2019).
date_created: 2019-12-20T12:22:57Z
date_published: 2019-12-17T00:00:00Z
date_updated: 2023-09-07T13:18:51Z
day: '17'
ddc:
- '570'
department:
- _id: MaLo
- _id: BjHo
doi: 10.1038/s41467-019-13702-4
ec_funded: 1
external_id:
isi:
- '000503009300001'
file:
- access_level: open_access
checksum: a1b44b427ba341383197790d0e8789fa
content_type: application/pdf
creator: dernst
date_created: 2019-12-23T07:34:56Z
date_updated: 2020-07-14T12:47:53Z
file_id: '7208'
file_name: 2019_NatureComm_Caldas.pdf
file_size: 8488733
relation: main_file
file_date_updated: 2020-07-14T12:47:53Z
has_accepted_license: '1'
intvolume: ' 10'
isi: 1
language:
- iso: eng
month: '12'
oa: 1
oa_version: Published Version
project:
- _id: 2595697A-B435-11E9-9278-68D0E5697425
call_identifier: H2020
grant_number: '679239'
name: Self-Organization of the Bacterial Cell
- _id: 260D98C8-B435-11E9-9278-68D0E5697425
name: Reconstitution of Bacterial Cell Division Using Purified Components
publication: Nature Communications
publication_identifier:
issn:
- 2041-1723
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
related_material:
record:
- id: '8358'
relation: dissertation_contains
status: public
scopus_import: '1'
status: public
title: Cooperative ordering of treadmilling filaments in cytoskeletal networks of
FtsZ and its crosslinker ZapA
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: c635000d-4b10-11ee-a964-aac5a93f6ac1
volume: 10
year: '2019'
...
---
_id: '629'
abstract:
- lang: eng
text: Even simple cells like bacteria have precisely regulated cellular anatomies,
which allow them to grow, divide and to respond to internal or external cues with
high fidelity. How spatial and temporal intracellular organization in prokaryotic
cells is achieved and maintained on the basis of locally interacting proteins
still remains largely a mystery. Bulk biochemical assays with purified components
and in vivo experiments help us to approach key cellular processes from two opposite
ends, in terms of minimal and maximal complexity. However, to understand how cellular
phenomena emerge, that are more than the sum of their parts, we have to assemble
cellular subsystems step by step from the bottom up. Here, we review recent in
vitro reconstitution experiments with proteins of the bacterial cell division
machinery and illustrate how they help to shed light on fundamental cellular mechanisms
that constitute spatiotemporal order and regulate cell division.
author:
- first_name: Martin
full_name: Loose, Martin
id: 462D4284-F248-11E8-B48F-1D18A9856A87
last_name: Loose
orcid: 0000-0001-7309-9724
- first_name: Katja
full_name: Zieske, Katja
last_name: Zieske
- first_name: Petra
full_name: Schwille, Petra
last_name: Schwille
citation:
ama: 'Loose M, Zieske K, Schwille P. Reconstitution of protein dynamics involved
in bacterial cell division. In: Prokaryotic Cytoskeletons. Vol 84. Sub-Cellular
Biochemistry. Springer; 2017:419-444. doi:10.1007/978-3-319-53047-5_15'
apa: Loose, M., Zieske, K., & Schwille, P. (2017). Reconstitution of protein
dynamics involved in bacterial cell division. In Prokaryotic Cytoskeletons
(Vol. 84, pp. 419–444). Springer. https://doi.org/10.1007/978-3-319-53047-5_15
chicago: Loose, Martin, Katja Zieske, and Petra Schwille. “Reconstitution of Protein
Dynamics Involved in Bacterial Cell Division.” In Prokaryotic Cytoskeletons,
84:419–44. Sub-Cellular Biochemistry. Springer, 2017. https://doi.org/10.1007/978-3-319-53047-5_15.
ieee: M. Loose, K. Zieske, and P. Schwille, “Reconstitution of protein dynamics
involved in bacterial cell division,” in Prokaryotic Cytoskeletons, vol.
84, Springer, 2017, pp. 419–444.
ista: 'Loose M, Zieske K, Schwille P. 2017.Reconstitution of protein dynamics involved
in bacterial cell division. In: Prokaryotic Cytoskeletons. vol. 84, 419–444.'
mla: Loose, Martin, et al. “Reconstitution of Protein Dynamics Involved in Bacterial
Cell Division.” Prokaryotic Cytoskeletons, vol. 84, Springer, 2017, pp.
419–44, doi:10.1007/978-3-319-53047-5_15.
short: M. Loose, K. Zieske, P. Schwille, in:, Prokaryotic Cytoskeletons, Springer,
2017, pp. 419–444.
date_created: 2018-12-11T11:47:35Z
date_published: 2017-05-13T00:00:00Z
date_updated: 2021-01-12T08:06:57Z
day: '13'
department:
- _id: MaLo
doi: 10.1007/978-3-319-53047-5_15
external_id:
pmid:
- '28500535'
intvolume: ' 84'
language:
- iso: eng
month: '05'
oa_version: None
page: 419 - 444
pmid: 1
publication: Prokaryotic Cytoskeletons
publication_identifier:
eisbn:
- 978-3-319-53047-5
publication_status: published
publisher: Springer
publist_id: '7165'
quality_controlled: '1'
scopus_import: 1
series_title: Sub-Cellular Biochemistry
status: public
title: Reconstitution of protein dynamics involved in bacterial cell division
type: book_chapter
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 84
year: '2017'
...
---
_id: '960'
abstract:
- lang: eng
text: The human cerebral cortex is the seat of our cognitive abilities and composed
of an extraordinary number of neurons, organized in six distinct layers. The establishment
of specific morphological and physiological features in individual neurons needs
to be regulated with high precision. Impairments in the sequential developmental
programs instructing corticogenesis lead to alterations in the cortical cytoarchitecture
which is thought to represent the major underlying cause for several neurological
disorders including neurodevelopmental and psychiatric diseases. In this review
we discuss the role of cell polarity at sequential stages during cortex development.
We first provide an overview of morphological cell polarity features in cortical
neural stem cells and newly-born postmitotic neurons. We then synthesize a conceptual
molecular and biochemical framework how cell polarity is established at the cellular
level through a break in symmetry in nascent cortical projection neurons. Lastly
we provide a perspective how the molecular mechanisms applying to single cells
could be probed and integrated in an in vivo and tissue-wide context.
article_number: '176'
article_processing_charge: Yes
author:
- first_name: Andi H
full_name: Hansen, Andi H
id: 38853E16-F248-11E8-B48F-1D18A9856A87
last_name: Hansen
- first_name: Christian F
full_name: Düllberg, Christian F
id: 459064DC-F248-11E8-B48F-1D18A9856A87
last_name: Düllberg
orcid: 0000-0001-6335-9748
- first_name: Christine
full_name: Mieck, Christine
id: 34CAE85C-F248-11E8-B48F-1D18A9856A87
last_name: Mieck
orcid: 0000-0003-1919-7416
- first_name: Martin
full_name: Loose, Martin
id: 462D4284-F248-11E8-B48F-1D18A9856A87
last_name: Loose
orcid: 0000-0001-7309-9724
- first_name: Simon
full_name: Hippenmeyer, Simon
id: 37B36620-F248-11E8-B48F-1D18A9856A87
last_name: Hippenmeyer
orcid: 0000-0003-2279-1061
citation:
ama: Hansen AH, Düllberg CF, Mieck C, Loose M, Hippenmeyer S. Cell polarity in cerebral
cortex development - cellular architecture shaped by biochemical networks. Frontiers
in Cellular Neuroscience. 2017;11. doi:10.3389/fncel.2017.00176
apa: Hansen, A. H., Düllberg, C. F., Mieck, C., Loose, M., & Hippenmeyer, S.
(2017). Cell polarity in cerebral cortex development - cellular architecture shaped
by biochemical networks. Frontiers in Cellular Neuroscience. Frontiers
Research Foundation. https://doi.org/10.3389/fncel.2017.00176
chicago: Hansen, Andi H, Christian F Düllberg, Christine Mieck, Martin Loose, and
Simon Hippenmeyer. “Cell Polarity in Cerebral Cortex Development - Cellular Architecture
Shaped by Biochemical Networks.” Frontiers in Cellular Neuroscience. Frontiers
Research Foundation, 2017. https://doi.org/10.3389/fncel.2017.00176.
ieee: A. H. Hansen, C. F. Düllberg, C. Mieck, M. Loose, and S. Hippenmeyer, “Cell
polarity in cerebral cortex development - cellular architecture shaped by biochemical
networks,” Frontiers in Cellular Neuroscience, vol. 11. Frontiers Research
Foundation, 2017.
ista: Hansen AH, Düllberg CF, Mieck C, Loose M, Hippenmeyer S. 2017. Cell polarity
in cerebral cortex development - cellular architecture shaped by biochemical networks.
Frontiers in Cellular Neuroscience. 11, 176.
mla: Hansen, Andi H., et al. “Cell Polarity in Cerebral Cortex Development - Cellular
Architecture Shaped by Biochemical Networks.” Frontiers in Cellular Neuroscience,
vol. 11, 176, Frontiers Research Foundation, 2017, doi:10.3389/fncel.2017.00176.
short: A.H. Hansen, C.F. Düllberg, C. Mieck, M. Loose, S. Hippenmeyer, Frontiers
in Cellular Neuroscience 11 (2017).
date_created: 2018-12-11T11:49:25Z
date_published: 2017-06-28T00:00:00Z
date_updated: 2024-03-25T23:30:23Z
day: '28'
ddc:
- '570'
department:
- _id: SiHi
- _id: MaLo
doi: 10.3389/fncel.2017.00176
ec_funded: 1
external_id:
isi:
- '000404486700001'
file:
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checksum: dc1f5a475b918d09a0f9f587400b1626
content_type: application/pdf
creator: system
date_created: 2018-12-12T10:09:40Z
date_updated: 2020-07-14T12:48:16Z
file_id: '4764'
file_name: IST-2017-830-v1+1_2017_Hansen_CellPolarity.pdf
file_size: 2153858
relation: main_file
file_date_updated: 2020-07-14T12:48:16Z
has_accepted_license: '1'
intvolume: ' 11'
isi: 1
language:
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month: '06'
oa: 1
oa_version: Published Version
project:
- _id: 25D61E48-B435-11E9-9278-68D0E5697425
call_identifier: FP7
grant_number: '618444'
name: Molecular Mechanisms of Cerebral Cortex Development
- _id: 25D7962E-B435-11E9-9278-68D0E5697425
grant_number: RGP0053/2014
name: Quantitative Structure-Function Analysis of Cerebral Cortex Assembly at Clonal
Level
- _id: 25681D80-B435-11E9-9278-68D0E5697425
call_identifier: FP7
grant_number: '291734'
name: International IST Postdoc Fellowship Programme
- _id: 25985A36-B435-11E9-9278-68D0E5697425
call_identifier: FWF
grant_number: T00817-B21
name: The biochemical basis of PAR polarization
publication: Frontiers in Cellular Neuroscience
publication_identifier:
issn:
- '16625102'
publication_status: published
publisher: Frontiers Research Foundation
publist_id: '6445'
pubrep_id: '830'
quality_controlled: '1'
related_material:
record:
- id: '9962'
relation: dissertation_contains
status: public
scopus_import: '1'
status: public
title: Cell polarity in cerebral cortex development - cellular architecture shaped
by biochemical networks
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: c635000d-4b10-11ee-a964-aac5a93f6ac1
volume: 11
year: '2017'
...
---
_id: '1213'
abstract:
- lang: eng
text: Bacterial cytokinesis is commonly initiated by the Z-ring, a dynamic cytoskeletal
structure that assembles at the site of division. Its primary component is FtsZ,
a tubulin-like GTPase, that like its eukaryotic relative forms protein filaments
in the presence of GTP. Since the discovery of the Z-ring 25 years ago, various
models for the role of FtsZ have been suggested. However, important information
about the architecture and dynamics of FtsZ filaments during cytokinesis is still
missing. One reason for this lack of knowledge has been the small size of bacteria,
which has made it difficult to resolve the orientation and dynamics of individual
FtsZ filaments in the Z-ring. While superresolution microscopy experiments have
helped to gain more information about the organization of the Z-ring in the dividing
cell, they were not yet able to elucidate a mechanism of how FtsZ filaments reorganize
during assembly and disassembly of the Z-ring. In this chapter, we explain how
to use an in vitro reconstitution approach to investigate the self-organization
of FtsZ filaments recruited to a biomimetic lipid bilayer by its membrane anchor
FtsA. We show how to perform single-molecule experiments to study the behavior
of individual FtsZ monomers during the constant reorganization of the FtsZ-FtsA
filament network. We describe how to analyze the dynamics of single molecules
and explain why this information can help to shed light onto possible mechanism
of Z-ring constriction. We believe that similar experimental approaches will be
useful to study the mechanism of membrane-based polymerization of other cytoskeletal
systems, not only from prokaryotic but also eukaryotic origin.
acknowledged_ssus:
- _id: Bio
acknowledgement: Natalia Baranova is supported by an EMBO Long-Term Fellowship (EMBO
ALTF 1163-2015) and Martin Loose by an ERC Starting Grant (ERCStG-2015-SelfOrganiCell).
alternative_title:
- Methods in Cell Biology
article_processing_charge: No
author:
- first_name: Natalia
full_name: Baranova, Natalia
id: 38661662-F248-11E8-B48F-1D18A9856A87
last_name: Baranova
orcid: 0000-0002-3086-9124
- first_name: Martin
full_name: Loose, Martin
id: 462D4284-F248-11E8-B48F-1D18A9856A87
last_name: Loose
orcid: 0000-0001-7309-9724
citation:
ama: 'Baranova NS, Loose M. Single-molecule measurements to study polymerization
dynamics of FtsZ-FtsA copolymers. In: Echard A, ed. Cytokinesis. Vol 137.
Academic Press; 2017:355-370. doi:10.1016/bs.mcb.2016.03.036'
apa: Baranova, N. S., & Loose, M. (2017). Single-molecule measurements to study
polymerization dynamics of FtsZ-FtsA copolymers. In A. Echard (Ed.), Cytokinesis
(Vol. 137, pp. 355–370). Academic Press. https://doi.org/10.1016/bs.mcb.2016.03.036
chicago: Baranova, Natalia S., and Martin Loose. “Single-Molecule Measurements to
Study Polymerization Dynamics of FtsZ-FtsA Copolymers.” In Cytokinesis,
edited by Arnaud Echard, 137:355–70. Academic Press, 2017. https://doi.org/10.1016/bs.mcb.2016.03.036.
ieee: N. S. Baranova and M. Loose, “Single-molecule measurements to study polymerization
dynamics of FtsZ-FtsA copolymers,” in Cytokinesis, vol. 137, A. Echard,
Ed. Academic Press, 2017, pp. 355–370.
ista: 'Baranova NS, Loose M. 2017.Single-molecule measurements to study polymerization
dynamics of FtsZ-FtsA copolymers. In: Cytokinesis. Methods in Cell Biology, vol.
137, 355–370.'
mla: Baranova, Natalia S., and Martin Loose. “Single-Molecule Measurements to Study
Polymerization Dynamics of FtsZ-FtsA Copolymers.” Cytokinesis, edited by
Arnaud Echard, vol. 137, Academic Press, 2017, pp. 355–70, doi:10.1016/bs.mcb.2016.03.036.
short: N.S. Baranova, M. Loose, in:, A. Echard (Ed.), Cytokinesis, Academic Press,
2017, pp. 355–370.
date_created: 2018-12-11T11:50:45Z
date_published: 2017-12-01T00:00:00Z
date_updated: 2023-09-20T11:16:30Z
day: '01'
department:
- _id: MaLo
doi: 10.1016/bs.mcb.2016.03.036
ec_funded: 1
editor:
- first_name: 'Arnaud '
full_name: 'Echard, Arnaud '
last_name: Echard
external_id:
isi:
- '000403542900022'
intvolume: ' 137'
isi: 1
language:
- iso: eng
month: '12'
oa_version: None
page: 355 - 370
project:
- _id: 2596EAB6-B435-11E9-9278-68D0E5697425
grant_number: ALTF 2015-1163
name: Synthesis of bacterial cell wall
- _id: 25681D80-B435-11E9-9278-68D0E5697425
call_identifier: FP7
grant_number: '291734'
name: International IST Postdoc Fellowship Programme
publication: Cytokinesis
publication_identifier:
issn:
- 0091679X
publication_status: published
publisher: Academic Press
publist_id: '6134'
quality_controlled: '1'
scopus_import: '1'
status: public
title: Single-molecule measurements to study polymerization dynamics of FtsZ-FtsA
copolymers
type: book_chapter
user_id: c635000d-4b10-11ee-a964-aac5a93f6ac1
volume: 137
year: '2017'
...