---
_id: '14826'
abstract:
- lang: eng
text: The plant-signaling molecule auxin triggers fast and slow cellular responses
across land plants and algae. The nuclear auxin pathway mediates gene expression
and controls growth and development in land plants, but this pathway is absent
from algal sister groups. Several components of rapid responses have been identified
in Arabidopsis, but it is unknown if these are part of a conserved mechanism.
We recently identified a fast, proteome-wide phosphorylation response to auxin.
Here, we show that this response occurs across 5 land plant and algal species
and converges on a core group of shared targets. We found conserved rapid physiological
responses to auxin in the same species and identified rapidly accelerated fibrosarcoma
(RAF)-like protein kinases as central mediators of auxin-triggered phosphorylation
across species. Genetic analysis connects this kinase to both auxin-triggered
protein phosphorylation and rapid cellular response, thus identifying an ancient
mechanism for fast auxin responses in the green lineage.
acknowledgement: 'We are grateful to Asuka Shitaku and Eri Koide for generating and
sharing the Marchantia PRAF-mCitrine line and Peng-Cheng Wang for sharing the Arabidopsis
raf mutant. We are grateful to our team members for discussions and helpful advice.
This work was supported by funding from the Netherlands Organization for Scientific
Research (NWO): VICI grant 865.14.001 and ENW-KLEIN OCENW.KLEIN.027 grants to D.W.;
VENI grant VI.VENI.212.003 to A.K.; the European Research Council AdG DIRNDL (contract
number 833867) to D.W.; CoG CATCH to J.S.; StG CELLONGATE (contract 803048) to M.F.;
and AdG ETAP (contract 742985) to J.F.; MEXT KAKENHI grant number JP19H05675 to
T.K.; JSPS KAKENHI grant number JP20H03275 to R.N.; Takeda Science Foundation to
R.N.; and the Austrian Science Fund (FWF, P29988) to J.F.'
article_processing_charge: Yes (in subscription journal)
article_type: original
author:
- first_name: Andre
full_name: Kuhn, Andre
last_name: Kuhn
- first_name: Mark
full_name: Roosjen, Mark
last_name: Roosjen
- first_name: Sumanth
full_name: Mutte, Sumanth
last_name: Mutte
- first_name: Shiv Mani
full_name: Dubey, Shiv Mani
last_name: Dubey
- first_name: Vanessa Polet
full_name: Carrillo Carrasco, Vanessa Polet
last_name: Carrillo Carrasco
- first_name: Sjef
full_name: Boeren, Sjef
last_name: Boeren
- first_name: Aline
full_name: Monzer, Aline
id: 2DB5D88C-D7B3-11E9-B8FD-7907E6697425
last_name: Monzer
- first_name: Jasper
full_name: Koehorst, Jasper
last_name: Koehorst
- first_name: Takayuki
full_name: Kohchi, Takayuki
last_name: Kohchi
- first_name: Ryuichi
full_name: Nishihama, Ryuichi
last_name: Nishihama
- first_name: Matyas
full_name: Fendrych, Matyas
id: 43905548-F248-11E8-B48F-1D18A9856A87
last_name: Fendrych
orcid: 0000-0002-9767-8699
- first_name: Joris
full_name: Sprakel, Joris
last_name: Sprakel
- first_name: Jiří
full_name: Friml, Jiří
id: 4159519E-F248-11E8-B48F-1D18A9856A87
last_name: Friml
orcid: 0000-0002-8302-7596
- first_name: Dolf
full_name: Weijers, Dolf
last_name: Weijers
citation:
ama: Kuhn A, Roosjen M, Mutte S, et al. RAF-like protein kinases mediate a deeply
conserved, rapid auxin response. Cell. 2024;187(1):130-148.e17. doi:10.1016/j.cell.2023.11.021
apa: Kuhn, A., Roosjen, M., Mutte, S., Dubey, S. M., Carrillo Carrasco, V. P., Boeren,
S., … Weijers, D. (2024). RAF-like protein kinases mediate a deeply conserved,
rapid auxin response. Cell. Elsevier. https://doi.org/10.1016/j.cell.2023.11.021
chicago: Kuhn, Andre, Mark Roosjen, Sumanth Mutte, Shiv Mani Dubey, Vanessa Polet
Carrillo Carrasco, Sjef Boeren, Aline Monzer, et al. “RAF-like Protein Kinases
Mediate a Deeply Conserved, Rapid Auxin Response.” Cell. Elsevier, 2024.
https://doi.org/10.1016/j.cell.2023.11.021.
ieee: A. Kuhn et al., “RAF-like protein kinases mediate a deeply conserved,
rapid auxin response,” Cell, vol. 187, no. 1. Elsevier, p. 130–148.e17,
2024.
ista: Kuhn A, Roosjen M, Mutte S, Dubey SM, Carrillo Carrasco VP, Boeren S, Monzer
A, Koehorst J, Kohchi T, Nishihama R, Fendrych M, Sprakel J, Friml J, Weijers
D. 2024. RAF-like protein kinases mediate a deeply conserved, rapid auxin response.
Cell. 187(1), 130–148.e17.
mla: Kuhn, Andre, et al. “RAF-like Protein Kinases Mediate a Deeply Conserved, Rapid
Auxin Response.” Cell, vol. 187, no. 1, Elsevier, 2024, p. 130–148.e17,
doi:10.1016/j.cell.2023.11.021.
short: A. Kuhn, M. Roosjen, S. Mutte, S.M. Dubey, V.P. Carrillo Carrasco, S. Boeren,
A. Monzer, J. Koehorst, T. Kohchi, R. Nishihama, M. Fendrych, J. Sprakel, J. Friml,
D. Weijers, Cell 187 (2024) 130–148.e17.
date_created: 2024-01-17T12:45:40Z
date_published: 2024-01-04T00:00:00Z
date_updated: 2024-01-22T13:43:40Z
day: '04'
ddc:
- '580'
department:
- _id: JiFr
doi: 10.1016/j.cell.2023.11.021
ec_funded: 1
external_id:
pmid:
- '38128538'
file:
- access_level: open_access
checksum: 06fd236a9ee0b46ccb05f44695bfc34b
content_type: application/pdf
creator: dernst
date_created: 2024-01-22T13:41:41Z
date_updated: 2024-01-22T13:41:41Z
file_id: '14874'
file_name: 2024_Cell_Kuhn.pdf
file_size: 13194060
relation: main_file
success: 1
file_date_updated: 2024-01-22T13:41:41Z
has_accepted_license: '1'
intvolume: ' 187'
issue: '1'
keyword:
- General Biochemistry
- Genetics and Molecular Biology
language:
- iso: eng
month: '01'
oa: 1
oa_version: Published Version
page: 130-148.e17
pmid: 1
project:
- _id: 261099A6-B435-11E9-9278-68D0E5697425
call_identifier: H2020
grant_number: '742985'
name: Tracing Evolution of Auxin Transport and Polarity in Plants
- _id: 262EF96E-B435-11E9-9278-68D0E5697425
call_identifier: FWF
grant_number: P29988
name: RNA-directed DNA methylation in plant development
publication: Cell
publication_identifier:
eissn:
- 1097-4172
issn:
- 0092-8674
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: RAF-like protein kinases mediate a deeply conserved, rapid auxin response
tmp:
image: /images/cc_by_nc.png
legal_code_url: https://creativecommons.org/licenses/by-nc/4.0/legalcode
name: Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0)
short: CC BY-NC (4.0)
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 187
year: '2024'
...
---
_id: '12802'
abstract:
- lang: eng
text: Little is known about the critical metabolic changes that neural cells have
to undergo during development and how temporary shifts in this program can influence
brain circuitries and behavior. Inspired by the discovery that mutations in SLC7A5,
a transporter of metabolically essential large neutral amino acids (LNAAs), lead
to autism, we employed metabolomic profiling to study the metabolic states of
the cerebral cortex across different developmental stages. We found that the forebrain
undergoes significant metabolic remodeling throughout development, with certain
groups of metabolites showing stage-specific changes, but what are the consequences
of perturbing this metabolic program? By manipulating Slc7a5 expression in neural
cells, we found that the metabolism of LNAAs and lipids are interconnected in
the cortex. Deletion of Slc7a5 in neurons affects the postnatal metabolic state,
leading to a shift in lipid metabolism. Additionally, it causes stage- and cell-type-specific
alterations in neuronal activity patterns, resulting in a long-term circuit dysfunction.
acknowledged_ssus:
- _id: PreCl
- _id: EM-Fac
- _id: Bio
- _id: LifeSc
acknowledgement: We thank A. Freeman and V. Voronin for technical assistance, S. Deixler,
A. Stichelberger, M. Schunn, and the Preclinical Facility for managing our animal
colony. We thank L. Andersen and J. Sonntag, who were involved in generating the
MADM lines. We thank the ISTA LSF Mass Spectrometry Core Facility for assistance
with the proteomic analysis, as well as the ISTA electron microscopy and Imaging
and Optics facility for technical support. Metabolomics LC-MS/MS analysis was performed
by the Metabolomics Facility at Vienna BioCenter Core Facilities (VBCF). We acknowledge
the support of the EMBL Metabolomics Core Facility (MCF) for lipidomics and intracellular
metabolomics mass spectrometry data acquisition and analysis. RNA sequencing was
performed by the Next Generation Sequencing Facility at VBCF. Schematics were generated
using Biorender.com. This work was supported by the Austrian Science Fund (FWF,
DK W1232-B24) and by the European Union’s Horizon 2020 research and innovation program
(ERC) grant 725780 (LinPro) to S.H. and 715508 (REVERSEAUTISM) to G.N.
article_processing_charge: Yes (via OA deal)
article_type: original
author:
- first_name: Lisa
full_name: Knaus, Lisa
id: 3B2ABCF4-F248-11E8-B48F-1D18A9856A87
last_name: Knaus
- first_name: Bernadette
full_name: Basilico, Bernadette
id: 36035796-5ACA-11E9-A75E-7AF2E5697425
last_name: Basilico
orcid: 0000-0003-1843-3173
- first_name: Daniel
full_name: Malzl, Daniel
last_name: Malzl
- first_name: Maria
full_name: Gerykova Bujalkova, Maria
last_name: Gerykova Bujalkova
- first_name: Mateja
full_name: Smogavec, Mateja
last_name: Smogavec
- first_name: Lena A.
full_name: Schwarz, Lena A.
last_name: Schwarz
- first_name: Sarah
full_name: Gorkiewicz, Sarah
id: f141a35d-15a9-11ec-9fb2-fef6becc7b6f
last_name: Gorkiewicz
- first_name: Nicole
full_name: Amberg, Nicole
id: 4CD6AAC6-F248-11E8-B48F-1D18A9856A87
last_name: Amberg
orcid: 0000-0002-3183-8207
- first_name: Florian
full_name: Pauler, Florian
id: 48EA0138-F248-11E8-B48F-1D18A9856A87
last_name: Pauler
orcid: 0000-0002-7462-0048
- first_name: Christian
full_name: Knittl-Frank, Christian
last_name: Knittl-Frank
- first_name: Marianna
full_name: Tassinari, Marianna
id: 7af593f1-d44a-11ed-bf94-a3646a6bb35e
last_name: Tassinari
- first_name: Nuno
full_name: Maulide, Nuno
last_name: Maulide
- first_name: Thomas
full_name: Rülicke, Thomas
last_name: Rülicke
- first_name: Jörg
full_name: Menche, Jörg
last_name: Menche
- first_name: Simon
full_name: Hippenmeyer, Simon
id: 37B36620-F248-11E8-B48F-1D18A9856A87
last_name: Hippenmeyer
orcid: 0000-0003-2279-1061
- first_name: Gaia
full_name: Novarino, Gaia
id: 3E57A680-F248-11E8-B48F-1D18A9856A87
last_name: Novarino
orcid: 0000-0002-7673-7178
citation:
ama: Knaus L, Basilico B, Malzl D, et al. Large neutral amino acid levels tune perinatal
neuronal excitability and survival. Cell. 2023;186(9):1950-1967.e25. doi:10.1016/j.cell.2023.02.037
apa: Knaus, L., Basilico, B., Malzl, D., Gerykova Bujalkova, M., Smogavec, M., Schwarz,
L. A., … Novarino, G. (2023). Large neutral amino acid levels tune perinatal neuronal
excitability and survival. Cell. Elsevier. https://doi.org/10.1016/j.cell.2023.02.037
chicago: Knaus, Lisa, Bernadette Basilico, Daniel Malzl, Maria Gerykova Bujalkova,
Mateja Smogavec, Lena A. Schwarz, Sarah Gorkiewicz, et al. “Large Neutral Amino
Acid Levels Tune Perinatal Neuronal Excitability and Survival.” Cell. Elsevier,
2023. https://doi.org/10.1016/j.cell.2023.02.037.
ieee: L. Knaus et al., “Large neutral amino acid levels tune perinatal neuronal
excitability and survival,” Cell, vol. 186, no. 9. Elsevier, p. 1950–1967.e25,
2023.
ista: Knaus L, Basilico B, Malzl D, Gerykova Bujalkova M, Smogavec M, Schwarz LA,
Gorkiewicz S, Amberg N, Pauler F, Knittl-Frank C, Tassinari M, Maulide N, Rülicke
T, Menche J, Hippenmeyer S, Novarino G. 2023. Large neutral amino acid levels
tune perinatal neuronal excitability and survival. Cell. 186(9), 1950–1967.e25.
mla: Knaus, Lisa, et al. “Large Neutral Amino Acid Levels Tune Perinatal Neuronal
Excitability and Survival.” Cell, vol. 186, no. 9, Elsevier, 2023, p. 1950–1967.e25,
doi:10.1016/j.cell.2023.02.037.
short: L. Knaus, B. Basilico, D. Malzl, M. Gerykova Bujalkova, M. Smogavec, L.A.
Schwarz, S. Gorkiewicz, N. Amberg, F. Pauler, C. Knittl-Frank, M. Tassinari, N.
Maulide, T. Rülicke, J. Menche, S. Hippenmeyer, G. Novarino, Cell 186 (2023) 1950–1967.e25.
date_created: 2023-04-05T08:15:40Z
date_published: 2023-04-27T00:00:00Z
date_updated: 2024-02-07T08:03:32Z
day: '27'
ddc:
- '570'
department:
- _id: SiHi
- _id: GaNo
doi: 10.1016/j.cell.2023.02.037
ec_funded: 1
external_id:
isi:
- '000991468700001'
file:
- access_level: open_access
checksum: 47e94fbe19e86505b429cb7a5b503ce6
content_type: application/pdf
creator: dernst
date_created: 2023-05-02T09:26:21Z
date_updated: 2023-05-02T09:26:21Z
file_id: '12889'
file_name: 2023_Cell_Knaus.pdf
file_size: 15712841
relation: main_file
success: 1
file_date_updated: 2023-05-02T09:26:21Z
has_accepted_license: '1'
intvolume: ' 186'
isi: 1
issue: '9'
keyword:
- General Biochemistry
- Genetics and Molecular Biology
language:
- iso: eng
month: '04'
oa: 1
oa_version: Published Version
page: 1950-1967.e25
project:
- _id: 2548AE96-B435-11E9-9278-68D0E5697425
call_identifier: FWF
grant_number: W1232-B24
name: Molecular Drug Targets
- _id: 260018B0-B435-11E9-9278-68D0E5697425
call_identifier: H2020
grant_number: '725780'
name: Principles of Neural Stem Cell Lineage Progression in Cerebral Cortex Development
- _id: 25444568-B435-11E9-9278-68D0E5697425
call_identifier: H2020
grant_number: '715508'
name: Probing the Reversibility of Autism Spectrum Disorders by Employing in vivo
and in vitro Models
publication: Cell
publication_identifier:
issn:
- 0092-8674
publication_status: published
publisher: Elsevier
quality_controlled: '1'
related_material:
link:
- description: News on ISTA Website
relation: press_release
url: https://ista.ac.at/en/news/feed-them-or-lose-them/
record:
- id: '13107'
relation: dissertation_contains
status: public
scopus_import: '1'
status: public
title: Large neutral amino acid levels tune perinatal neuronal excitability and survival
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: 186
year: '2023'
...
---
_id: '10573'
abstract:
- lang: eng
text: How tissues acquire complex shapes is a fundamental question in biology and
regenerative medicine. Zebrafish semicircular canals form from invaginations in
the otic epithelium (buds) that extend and fuse to form the hubs of each canal.
We find that conventional actomyosin-driven behaviors are not required. Instead,
local secretion of hyaluronan, made by the enzymes uridine 5′-diphosphate dehydrogenase
(ugdh) and hyaluronan synthase 3 (has3), drives canal morphogenesis. Charged hyaluronate
polymers osmotically swell with water and generate isotropic extracellular pressure
to deform the overlying epithelium into buds. The mechanical anisotropy needed
to shape buds into tubes is conferred by a polarized distribution of actomyosin
and E-cadherin-rich membrane tethers, which we term cytocinches. Most work on
tissue morphogenesis ascribes actomyosin contractility as the driving force, while
the extracellular matrix shapes tissues through differential stiffness. Our work
inverts this expectation. Hyaluronate pressure shaped by anisotropic tissue stiffness
may be a widespread mechanism for powering morphological change in organogenesis
and tissue engineering.
acknowledgement: We thank Ian Swinburne, Sandy Nandagopal, and Toru Kawanishi for
support, discussions, and reagents. We thank Vanessa Barone, Joseph Nasser, and
members of the Megason lab for useful comments on the manuscript and general feedback.
We are grateful to the Heisenberg and Knaut labs for transgenic fish. Diagrams on
the right in the graphical abstract were created using BioRender. This work was
supported by NIH R01DC015478 and NIH R01GM107733 to S.G.M. A.M. was supported by
Human Frontiers Science Program LTF and NIH K99HD098918.
article_processing_charge: No
article_type: original
author:
- first_name: Akankshi
full_name: Munjal, Akankshi
last_name: Munjal
- 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: Tony Y.C.
full_name: Tsai, Tony Y.C.
last_name: Tsai
- first_name: Timothy J.
full_name: Mitchison, Timothy J.
last_name: Mitchison
- first_name: Sean G.
full_name: Megason, Sean G.
last_name: Megason
citation:
ama: Munjal A, Hannezo EB, Tsai TYC, Mitchison TJ, Megason SG. Extracellular hyaluronate
pressure shaped by cellular tethers drives tissue morphogenesis. Cell.
2021;184(26):6313-6325.e18. doi:10.1016/j.cell.2021.11.025
apa: Munjal, A., Hannezo, E. B., Tsai, T. Y. C., Mitchison, T. J., & Megason,
S. G. (2021). Extracellular hyaluronate pressure shaped by cellular tethers drives
tissue morphogenesis. Cell. Elsevier ; Cell Press. https://doi.org/10.1016/j.cell.2021.11.025
chicago: Munjal, Akankshi, Edouard B Hannezo, Tony Y.C. Tsai, Timothy J. Mitchison,
and Sean G. Megason. “Extracellular Hyaluronate Pressure Shaped by Cellular Tethers
Drives Tissue Morphogenesis.” Cell. Elsevier ; Cell Press, 2021. https://doi.org/10.1016/j.cell.2021.11.025.
ieee: A. Munjal, E. B. Hannezo, T. Y. C. Tsai, T. J. Mitchison, and S. G. Megason,
“Extracellular hyaluronate pressure shaped by cellular tethers drives tissue morphogenesis,”
Cell, vol. 184, no. 26. Elsevier ; Cell Press, p. 6313–6325.e18, 2021.
ista: Munjal A, Hannezo EB, Tsai TYC, Mitchison TJ, Megason SG. 2021. Extracellular
hyaluronate pressure shaped by cellular tethers drives tissue morphogenesis. Cell.
184(26), 6313–6325.e18.
mla: Munjal, Akankshi, et al. “Extracellular Hyaluronate Pressure Shaped by Cellular
Tethers Drives Tissue Morphogenesis.” Cell, vol. 184, no. 26, Elsevier ;
Cell Press, 2021, p. 6313–6325.e18, doi:10.1016/j.cell.2021.11.025.
short: A. Munjal, E.B. Hannezo, T.Y.C. Tsai, T.J. Mitchison, S.G. Megason, Cell
184 (2021) 6313–6325.e18.
date_created: 2021-12-26T23:01:26Z
date_published: 2021-12-22T00:00:00Z
date_updated: 2023-08-17T06:28:25Z
day: '22'
department:
- _id: EdHa
doi: 10.1016/j.cell.2021.11.025
external_id:
isi:
- '000735387500002'
intvolume: ' 184'
isi: 1
issue: '26'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://www.biorxiv.org/content/10.1101/2020.09.28.316042
month: '12'
oa: 1
oa_version: Preprint
page: 6313-6325.e18
publication: Cell
publication_identifier:
eissn:
- 1097-4172
issn:
- 0092-8674
publication_status: published
publisher: Elsevier ; Cell Press
quality_controlled: '1'
scopus_import: '1'
status: public
title: Extracellular hyaluronate pressure shaped by cellular tethers drives tissue
morphogenesis
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 184
year: '2021'
...
---
_id: '10348'
abstract:
- lang: eng
text: The endosomal sorting complex required for transport-III (ESCRT-III) catalyzes
membrane fission from within membrane necks, a process that is essential for many
cellular functions, from cell division to lysosome degradation and autophagy.
How it breaks membranes, though, remains unknown. Here, we characterize a sequential
polymerization of ESCRT-III subunits that, driven by a recruitment cascade and
by continuous subunit-turnover powered by the ATPase Vps4, induces membrane deformation
and fission. During this process, the exchange of Vps24 for Did2 induces a tilt
in the polymer-membrane interface, which triggers transition from flat spiral
polymers to helical filament to drive the formation of membrane protrusions, and
ends with the formation of a highly constricted Did2-Ist1 co-polymer that we show
is competent to promote fission when bound on the inside of membrane necks. Overall,
our results suggest a mechanism of stepwise changes in ESCRT-III filament structure
and mechanical properties via exchange of the filament subunits to catalyze ESCRT-III
activity.
acknowledgement: The authors thank Nicolas Chiaruttini, Jean Gruenberg, and Lena Harker-Kirschneck
for careful correction of this manuscript and helpful discussions. The authors want
to thank the NCCR Chemical Biology for constant support during this project. A.R.
acknowledges funding from the Swiss National Fund for Research (31003A_130520, 31003A_149975,
and 31003A_173087) and the European Research Council Consolidator (311536). A.Š.
acknowledges the European Research Council (802960). B.B. thanks the BBSRC (BB/K009001/1)
and Wellcome Trust (203276/Z/16/Z) for support. J.M.v.F. acknowledges funding through
an EMBO Long-Term Fellowship (ALTF 1065-2015), the European Commission FP7 (Marie
Curie Actions, LTFCOFUND2013, and GA-2013-609409), and a Transitional Postdoc fellowship
(2015/345) from the Swiss SystemsX.ch initiative, evaluated by the Swiss National
Science Foundation and Swiss National Science Foundation Research (SNSF SINERGIA
160728/1 [leader, Sophie Martin]).
article_processing_charge: No
article_type: original
author:
- first_name: Anna-Katharina
full_name: Pfitzner, Anna-Katharina
last_name: Pfitzner
- first_name: Vincent
full_name: Mercier, Vincent
last_name: Mercier
- first_name: Xiuyun
full_name: Jiang, Xiuyun
last_name: Jiang
- first_name: Joachim
full_name: Moser von Filseck, Joachim
last_name: Moser von Filseck
- first_name: Buzz
full_name: Baum, Buzz
last_name: Baum
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
- first_name: Aurélien
full_name: Roux, Aurélien
last_name: Roux
citation:
ama: Pfitzner A-K, Mercier V, Jiang X, et al. An ESCRT-III polymerization sequence
drives membrane deformation and fission. Cell. 2020;182(5):1140-1155.e18.
doi:10.1016/j.cell.2020.07.021
apa: Pfitzner, A.-K., Mercier, V., Jiang, X., Moser von Filseck, J., Baum, B., Šarić,
A., & Roux, A. (2020). An ESCRT-III polymerization sequence drives membrane
deformation and fission. Cell. Elsevier. https://doi.org/10.1016/j.cell.2020.07.021
chicago: Pfitzner, Anna-Katharina, Vincent Mercier, Xiuyun Jiang, Joachim Moser
von Filseck, Buzz Baum, Anđela Šarić, and Aurélien Roux. “An ESCRT-III Polymerization
Sequence Drives Membrane Deformation and Fission.” Cell. Elsevier, 2020.
https://doi.org/10.1016/j.cell.2020.07.021.
ieee: A.-K. Pfitzner et al., “An ESCRT-III polymerization sequence drives
membrane deformation and fission,” Cell, vol. 182, no. 5. Elsevier, p.
1140–1155.e18, 2020.
ista: Pfitzner A-K, Mercier V, Jiang X, Moser von Filseck J, Baum B, Šarić A, Roux
A. 2020. An ESCRT-III polymerization sequence drives membrane deformation and
fission. Cell. 182(5), 1140–1155.e18.
mla: Pfitzner, Anna-Katharina, et al. “An ESCRT-III Polymerization Sequence Drives
Membrane Deformation and Fission.” Cell, vol. 182, no. 5, Elsevier, 2020,
p. 1140–1155.e18, doi:10.1016/j.cell.2020.07.021.
short: A.-K. Pfitzner, V. Mercier, X. Jiang, J. Moser von Filseck, B. Baum, A. Šarić,
A. Roux, Cell 182 (2020) 1140–1155.e18.
date_created: 2021-11-26T08:02:27Z
date_published: 2020-08-18T00:00:00Z
date_updated: 2021-11-26T08:58:37Z
day: '18'
doi: 10.1016/j.cell.2020.07.021
extern: '1'
external_id:
pmid:
- '32814015'
intvolume: ' 182'
issue: '5'
keyword:
- general biochemistry
- genetics and molecular biology
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://www.sciencedirect.com/science/article/pii/S0092867420309296
month: '08'
oa: 1
oa_version: Published Version
page: 1140-1155.e18
pmid: 1
publication: Cell
publication_identifier:
issn:
- 0092-8674
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: An ESCRT-III polymerization sequence drives membrane deformation and fission
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 182
year: '2020'
...
---
_id: '6877'
article_processing_charge: No
article_type: original
author:
- first_name: Aglaja
full_name: Kopf, Aglaja
id: 31DAC7B6-F248-11E8-B48F-1D18A9856A87
last_name: Kopf
orcid: 0000-0002-2187-6656
- first_name: Michael K
full_name: Sixt, Michael K
id: 41E9FBEA-F248-11E8-B48F-1D18A9856A87
last_name: Sixt
orcid: 0000-0002-6620-9179
citation:
ama: Kopf A, Sixt MK. The neural crest pitches in to remove apoptotic debris. Cell.
2019;179(1):51-53. doi:10.1016/j.cell.2019.08.047
apa: Kopf, A., & Sixt, M. K. (2019). The neural crest pitches in to remove apoptotic
debris. Cell. Elsevier. https://doi.org/10.1016/j.cell.2019.08.047
chicago: Kopf, Aglaja, and Michael K Sixt. “The Neural Crest Pitches in to Remove
Apoptotic Debris.” Cell. Elsevier, 2019. https://doi.org/10.1016/j.cell.2019.08.047.
ieee: A. Kopf and M. K. Sixt, “The neural crest pitches in to remove apoptotic debris,”
Cell, vol. 179, no. 1. Elsevier, pp. 51–53, 2019.
ista: Kopf A, Sixt MK. 2019. The neural crest pitches in to remove apoptotic debris.
Cell. 179(1), 51–53.
mla: Kopf, Aglaja, and Michael K. Sixt. “The Neural Crest Pitches in to Remove Apoptotic
Debris.” Cell, vol. 179, no. 1, Elsevier, 2019, pp. 51–53, doi:10.1016/j.cell.2019.08.047.
short: A. Kopf, M.K. Sixt, Cell 179 (2019) 51–53.
date_created: 2019-09-15T22:00:46Z
date_published: 2019-09-19T00:00:00Z
date_updated: 2024-03-25T23:30:22Z
day: '19'
department:
- _id: MiSi
doi: 10.1016/j.cell.2019.08.047
external_id:
isi:
- '000486618500011'
pmid:
- '31539498'
intvolume: ' 179'
isi: 1
issue: '1'
language:
- iso: eng
month: '09'
oa_version: None
page: 51-53
pmid: 1
publication: Cell
publication_identifier:
eissn:
- 1097-4172
issn:
- 0092-8674
publication_status: published
publisher: Elsevier
quality_controlled: '1'
related_material:
record:
- id: '6891'
relation: dissertation_contains
status: public
scopus_import: '1'
status: public
title: The neural crest pitches in to remove apoptotic debris
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 179
year: '2019'
...
---
_id: '7001'
acknowledged_ssus:
- _id: PreCl
- _id: Bio
article_processing_charge: No
article_type: original
author:
- first_name: Cornelia
full_name: Schwayer, Cornelia
id: 3436488C-F248-11E8-B48F-1D18A9856A87
last_name: Schwayer
orcid: 0000-0001-5130-2226
- first_name: Shayan
full_name: Shamipour, Shayan
id: 40B34FE2-F248-11E8-B48F-1D18A9856A87
last_name: Shamipour
- first_name: Kornelija
full_name: Pranjic-Ferscha, Kornelija
id: 4362B3C2-F248-11E8-B48F-1D18A9856A87
last_name: Pranjic-Ferscha
- first_name: Alexandra
full_name: Schauer, Alexandra
id: 30A536BA-F248-11E8-B48F-1D18A9856A87
last_name: Schauer
orcid: 0000-0001-7659-9142
- first_name: M
full_name: Balda, M
last_name: Balda
- first_name: M
full_name: Tada, M
last_name: Tada
- first_name: K
full_name: Matter, K
last_name: Matter
- 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: Schwayer C, Shamipour S, Pranjic-Ferscha K, et al. Mechanosensation of tight
junctions depends on ZO-1 phase separation and flow. Cell. 2019;179(4):937-952.e18.
doi:10.1016/j.cell.2019.10.006
apa: Schwayer, C., Shamipour, S., Pranjic-Ferscha, K., Schauer, A., Balda, M., Tada,
M., … Heisenberg, C.-P. J. (2019). Mechanosensation of tight junctions depends
on ZO-1 phase separation and flow. Cell. Cell Press. https://doi.org/10.1016/j.cell.2019.10.006
chicago: Schwayer, Cornelia, Shayan Shamipour, Kornelija Pranjic-Ferscha, Alexandra
Schauer, M Balda, M Tada, K Matter, and Carl-Philipp J Heisenberg. “Mechanosensation
of Tight Junctions Depends on ZO-1 Phase Separation and Flow.” Cell. Cell
Press, 2019. https://doi.org/10.1016/j.cell.2019.10.006.
ieee: C. Schwayer et al., “Mechanosensation of tight junctions depends on
ZO-1 phase separation and flow,” Cell, vol. 179, no. 4. Cell Press, p.
937–952.e18, 2019.
ista: Schwayer C, Shamipour S, Pranjic-Ferscha K, Schauer A, Balda M, Tada M, Matter
K, Heisenberg C-PJ. 2019. Mechanosensation of tight junctions depends on ZO-1
phase separation and flow. Cell. 179(4), 937–952.e18.
mla: Schwayer, Cornelia, et al. “Mechanosensation of Tight Junctions Depends on
ZO-1 Phase Separation and Flow.” Cell, vol. 179, no. 4, Cell Press, 2019,
p. 937–952.e18, doi:10.1016/j.cell.2019.10.006.
short: C. Schwayer, S. Shamipour, K. Pranjic-Ferscha, A. Schauer, M. Balda, M. Tada,
K. Matter, C.-P.J. Heisenberg, Cell 179 (2019) 937–952.e18.
date_created: 2019-11-12T12:51:06Z
date_published: 2019-10-31T00:00:00Z
date_updated: 2024-03-25T23:30:21Z
day: '31'
ddc:
- '570'
department:
- _id: CaHe
- _id: BjHo
doi: 10.1016/j.cell.2019.10.006
ec_funded: 1
external_id:
isi:
- '000493898000012'
pmid:
- '31675500'
file:
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content_type: application/pdf
creator: dernst
date_created: 2020-10-21T07:09:45Z
date_updated: 2020-10-21T07:09:45Z
file_id: '8684'
file_name: 2019_Cell_Schwayer_accepted.pdf
file_size: 8805878
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oa_version: Submitted Version
page: 937-952.e18
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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: Cell
publication_identifier:
eissn:
- 1097-4172
issn:
- 0092-8674
publication_status: published
publisher: Cell Press
quality_controlled: '1'
related_material:
link:
- description: News auf IST Website
relation: press_release
url: https://ist.ac.at/en/news/biochemistry-meets-mechanics-the-sensitive-nature-of-cell-cell-contact-formation-in-embryo-development/
record:
- id: '7186'
relation: dissertation_contains
status: public
- id: '8350'
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status: public
scopus_import: '1'
status: public
title: Mechanosensation of tight junctions depends on ZO-1 phase separation and flow
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 179
year: '2019'
...
---
_id: '8436'
abstract:
- lang: eng
text: The exchange of metabolites between the mitochondrial matrix and the cytosol
depends on β-barrel channels in the outer membrane and α-helical carrier proteins
in the inner membrane. The essential translocase of the inner membrane (TIM) chaperones
escort these proteins through the intermembrane space, but the structural and
mechanistic details remain elusive. We have used an integrated structural biology
approach to reveal the functional principle of TIM chaperones. Multiple clamp-like
binding sites hold the mitochondrial membrane proteins in a translocation-competent
elongated form, thus mimicking characteristics of co-translational membrane insertion.
The bound preprotein undergoes conformational dynamics within the chaperone binding
clefts, pointing to a multitude of dynamic local binding events. Mutations in
these binding sites cause cell death or growth defects associated with impairment
of carrier and β-barrel protein biogenesis. Our work reveals how a single mitochondrial
“transfer-chaperone” system is able to guide α-helical and β-barrel membrane proteins
in a “nascent chain-like” conformation through a ribosome-free compartment.
article_processing_charge: No
article_type: original
author:
- first_name: Katharina
full_name: Weinhäupl, Katharina
last_name: Weinhäupl
- first_name: Caroline
full_name: Lindau, Caroline
last_name: Lindau
- first_name: Audrey
full_name: Hessel, Audrey
last_name: Hessel
- first_name: Yong
full_name: Wang, Yong
last_name: Wang
- first_name: Conny
full_name: Schütze, Conny
last_name: Schütze
- first_name: Tobias
full_name: Jores, Tobias
last_name: Jores
- first_name: Laura
full_name: Melchionda, Laura
last_name: Melchionda
- first_name: Birgit
full_name: Schönfisch, Birgit
last_name: Schönfisch
- first_name: Hubert
full_name: Kalbacher, Hubert
last_name: Kalbacher
- first_name: Beate
full_name: Bersch, Beate
last_name: Bersch
- first_name: Doron
full_name: Rapaport, Doron
last_name: Rapaport
- first_name: Martha
full_name: Brennich, Martha
last_name: Brennich
- first_name: Kresten
full_name: Lindorff-Larsen, Kresten
last_name: Lindorff-Larsen
- first_name: Nils
full_name: Wiedemann, Nils
last_name: Wiedemann
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
citation:
ama: Weinhäupl K, Lindau C, Hessel A, et al. Structural basis of membrane protein
chaperoning through the mitochondrial intermembrane space. Cell. 2018;175(5):1365-1379.e25.
doi:10.1016/j.cell.2018.10.039
apa: Weinhäupl, K., Lindau, C., Hessel, A., Wang, Y., Schütze, C., Jores, T., …
Schanda, P. (2018). Structural basis of membrane protein chaperoning through the
mitochondrial intermembrane space. Cell. Elsevier. https://doi.org/10.1016/j.cell.2018.10.039
chicago: Weinhäupl, Katharina, Caroline Lindau, Audrey Hessel, Yong Wang, Conny
Schütze, Tobias Jores, Laura Melchionda, et al. “Structural Basis of Membrane
Protein Chaperoning through the Mitochondrial Intermembrane Space.” Cell.
Elsevier, 2018. https://doi.org/10.1016/j.cell.2018.10.039.
ieee: K. Weinhäupl et al., “Structural basis of membrane protein chaperoning
through the mitochondrial intermembrane space,” Cell, vol. 175, no. 5.
Elsevier, p. 1365–1379.e25, 2018.
ista: Weinhäupl K, Lindau C, Hessel A, Wang Y, Schütze C, Jores T, Melchionda L,
Schönfisch B, Kalbacher H, Bersch B, Rapaport D, Brennich M, Lindorff-Larsen K,
Wiedemann N, Schanda P. 2018. Structural basis of membrane protein chaperoning
through the mitochondrial intermembrane space. Cell. 175(5), 1365–1379.e25.
mla: Weinhäupl, Katharina, et al. “Structural Basis of Membrane Protein Chaperoning
through the Mitochondrial Intermembrane Space.” Cell, vol. 175, no. 5,
Elsevier, 2018, p. 1365–1379.e25, doi:10.1016/j.cell.2018.10.039.
short: K. Weinhäupl, C. Lindau, A. Hessel, Y. Wang, C. Schütze, T. Jores, L. Melchionda,
B. Schönfisch, H. Kalbacher, B. Bersch, D. Rapaport, M. Brennich, K. Lindorff-Larsen,
N. Wiedemann, P. Schanda, Cell 175 (2018) 1365–1379.e25.
date_created: 2020-09-18T10:04:39Z
date_published: 2018-11-15T00:00:00Z
date_updated: 2021-01-12T08:19:15Z
day: '15'
doi: 10.1016/j.cell.2018.10.039
extern: '1'
intvolume: ' 175'
issue: '5'
keyword:
- General Biochemistry
- Genetics and Molecular Biology
language:
- iso: eng
month: '11'
oa_version: None
page: 1365-1379.e25
publication: Cell
publication_identifier:
issn:
- 0092-8674
publication_status: published
publisher: Elsevier
quality_controlled: '1'
status: public
title: Structural basis of membrane protein chaperoning through the mitochondrial
intermembrane space
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 175
year: '2018'
...
---
_id: '11073'
abstract:
- lang: eng
text: Human cancer cells bear complex chromosome rearrangements that can be potential
drivers of cancer development. However, the molecular mechanisms underlying these
rearrangements have been unclear. Zhang et al. use a new technique combining live-cell
imaging and single-cell sequencing to demonstrate that chromosomes mis-segregated
to micronuclei frequently undergo chromothripsis-like rearrangements in the subsequent
cell cycle.
article_processing_charge: No
article_type: original
author:
- first_name: Emily M.
full_name: Hatch, Emily M.
last_name: Hatch
- first_name: Martin W
full_name: HETZER, Martin W
id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed
last_name: HETZER
orcid: 0000-0002-2111-992X
citation:
ama: Hatch EM, Hetzer M. Linking micronuclei to chromosome fragmentation. Cell.
2015;161(7):1502-1504. doi:10.1016/j.cell.2015.06.005
apa: Hatch, E. M., & Hetzer, M. (2015). Linking micronuclei to chromosome fragmentation.
Cell. Elsevier. https://doi.org/10.1016/j.cell.2015.06.005
chicago: Hatch, Emily M., and Martin Hetzer. “Linking Micronuclei to Chromosome
Fragmentation.” Cell. Elsevier, 2015. https://doi.org/10.1016/j.cell.2015.06.005.
ieee: E. M. Hatch and M. Hetzer, “Linking micronuclei to chromosome fragmentation,”
Cell, vol. 161, no. 7. Elsevier, pp. 1502–1504, 2015.
ista: Hatch EM, Hetzer M. 2015. Linking micronuclei to chromosome fragmentation.
Cell. 161(7), 1502–1504.
mla: Hatch, Emily M., and Martin Hetzer. “Linking Micronuclei to Chromosome Fragmentation.”
Cell, vol. 161, no. 7, Elsevier, 2015, pp. 1502–04, doi:10.1016/j.cell.2015.06.005.
short: E.M. Hatch, M. Hetzer, Cell 161 (2015) 1502–1504.
date_created: 2022-04-07T07:48:49Z
date_published: 2015-06-18T00:00:00Z
date_updated: 2022-07-18T08:34:33Z
day: '18'
doi: 10.1016/j.cell.2015.06.005
extern: '1'
external_id:
pmid:
- '26091034'
intvolume: ' 161'
issue: '7'
keyword:
- General Biochemistry
- Genetics and Molecular Biology
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1016/j.cell.2015.06.005
month: '06'
oa: 1
oa_version: Published Version
page: 1502-1504
pmid: 1
publication: Cell
publication_identifier:
issn:
- 0092-8674
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: Linking micronuclei to chromosome fragmentation
type: journal_article
user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd
volume: 161
year: '2015'
...
---
_id: '11080'
abstract:
- lang: eng
text: The spindle assembly checkpoint prevents separation of sister chromatids until
each kinetochore is attached to the mitotic spindle. Rodriguez-Bravo et al. report
that the nuclear pore complex scaffolds spindle assembly checkpoint signaling
in interphase, providing a store of inhibitory signals that limits the speed of
the subsequent mitosis.
article_processing_charge: No
article_type: original
author:
- first_name: Abigail
full_name: Buchwalter, Abigail
last_name: Buchwalter
- first_name: Martin W
full_name: HETZER, Martin W
id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed
last_name: HETZER
orcid: 0000-0002-2111-992X
citation:
ama: Buchwalter A, Hetzer M. Nuclear pores set the speed limit for mitosis. Cell.
2014;156(5):868-869. doi:10.1016/j.cell.2014.02.004
apa: Buchwalter, A., & Hetzer, M. (2014). Nuclear pores set the speed limit
for mitosis. Cell. Elsevier. https://doi.org/10.1016/j.cell.2014.02.004
chicago: Buchwalter, Abigail, and Martin Hetzer. “Nuclear Pores Set the Speed Limit
for Mitosis.” Cell. Elsevier, 2014. https://doi.org/10.1016/j.cell.2014.02.004.
ieee: A. Buchwalter and M. Hetzer, “Nuclear pores set the speed limit for mitosis,”
Cell, vol. 156, no. 5. Elsevier, pp. 868–869, 2014.
ista: Buchwalter A, Hetzer M. 2014. Nuclear pores set the speed limit for mitosis.
Cell. 156(5), 868–869.
mla: Buchwalter, Abigail, and Martin Hetzer. “Nuclear Pores Set the Speed Limit
for Mitosis.” Cell, vol. 156, no. 5, Elsevier, 2014, pp. 868–69, doi:10.1016/j.cell.2014.02.004.
short: A. Buchwalter, M. Hetzer, Cell 156 (2014) 868–869.
date_created: 2022-04-07T07:50:04Z
date_published: 2014-02-27T00:00:00Z
date_updated: 2022-07-18T08:44:33Z
day: '27'
doi: 10.1016/j.cell.2014.02.004
extern: '1'
external_id:
pmid:
- '24581486'
intvolume: ' 156'
issue: '5'
keyword:
- General Biochemistry
- Genetics and Molecular Biology
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1016/j.cell.2014.02.004
month: '02'
oa: 1
oa_version: Published Version
page: 868-869
pmid: 1
publication: Cell
publication_identifier:
issn:
- 0092-8674
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: Nuclear pores set the speed limit for mitosis
type: journal_article
user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd
volume: 156
year: '2014'
...
---
_id: '6122'
author:
- first_name: Gerit A.
full_name: Linneweber, Gerit A.
last_name: Linneweber
- first_name: Jake
full_name: Jacobson, Jake
last_name: Jacobson
- first_name: Karl Emanuel
full_name: Busch, Karl Emanuel
last_name: Busch
- first_name: Bruno
full_name: Hudry, Bruno
last_name: Hudry
- first_name: Christo P.
full_name: Christov, Christo P.
last_name: Christov
- first_name: Dirk
full_name: Dormann, Dirk
last_name: Dormann
- first_name: Michaela
full_name: Yuan, Michaela
last_name: Yuan
- first_name: Tomoki
full_name: Otani, Tomoki
last_name: Otani
- first_name: Elisabeth
full_name: Knust, Elisabeth
last_name: Knust
- first_name: Mario
full_name: de Bono, Mario
id: 4E3FF80E-F248-11E8-B48F-1D18A9856A87
last_name: de Bono
orcid: 0000-0001-8347-0443
- first_name: Irene
full_name: Miguel-Aliaga, Irene
last_name: Miguel-Aliaga
citation:
ama: Linneweber GA, Jacobson J, Busch KE, et al. Neuronal control of metabolism
through nutrient-dependent modulation of tracheal branching. Cell. 2014;156(1-2):69-83.
doi:10.1016/j.cell.2013.12.008
apa: Linneweber, G. A., Jacobson, J., Busch, K. E., Hudry, B., Christov, C. P.,
Dormann, D., … Miguel-Aliaga, I. (2014). Neuronal control of metabolism through
nutrient-dependent modulation of tracheal branching. Cell. Elsevier. https://doi.org/10.1016/j.cell.2013.12.008
chicago: Linneweber, Gerit A., Jake Jacobson, Karl Emanuel Busch, Bruno Hudry, Christo P.
Christov, Dirk Dormann, Michaela Yuan, et al. “Neuronal Control of Metabolism
through Nutrient-Dependent Modulation of Tracheal Branching.” Cell. Elsevier,
2014. https://doi.org/10.1016/j.cell.2013.12.008.
ieee: G. A. Linneweber et al., “Neuronal control of metabolism through nutrient-dependent
modulation of tracheal branching,” Cell, vol. 156, no. 1–2. Elsevier, pp.
69–83, 2014.
ista: Linneweber GA, Jacobson J, Busch KE, Hudry B, Christov CP, Dormann D, Yuan
M, Otani T, Knust E, de Bono M, Miguel-Aliaga I. 2014. Neuronal control of metabolism
through nutrient-dependent modulation of tracheal branching. Cell. 156(1–2), 69–83.
mla: Linneweber, Gerit A., et al. “Neuronal Control of Metabolism through Nutrient-Dependent
Modulation of Tracheal Branching.” Cell, vol. 156, no. 1–2, Elsevier, 2014,
pp. 69–83, doi:10.1016/j.cell.2013.12.008.
short: G.A. Linneweber, J. Jacobson, K.E. Busch, B. Hudry, C.P. Christov, D. Dormann,
M. Yuan, T. Otani, E. Knust, M. de Bono, I. Miguel-Aliaga, Cell 156 (2014) 69–83.
date_created: 2019-03-19T14:35:30Z
date_published: 2014-01-16T00:00:00Z
date_updated: 2021-01-12T08:06:13Z
day: '16'
ddc:
- '570'
doi: 10.1016/j.cell.2013.12.008
extern: '1'
external_id:
pmid:
- '24439370'
file:
- access_level: open_access
checksum: ad6ef68f37fb711d9abcd97fc06ad316
content_type: application/pdf
creator: kschuh
date_created: 2019-03-19T14:40:38Z
date_updated: 2020-07-14T12:47:20Z
file_id: '6123'
file_name: 2014_Elsevier_Linneweber.pdf
file_size: 5020084
relation: main_file
file_date_updated: 2020-07-14T12:47:20Z
has_accepted_license: '1'
intvolume: ' 156'
issue: 1-2
language:
- iso: eng
month: '01'
oa: 1
oa_version: Published Version
page: 69-83
pmid: 1
publication: Cell
publication_identifier:
issn:
- 0092-8674
publication_status: published
publisher: Elsevier
quality_controlled: '1'
status: public
title: Neuronal control of metabolism through nutrient-dependent modulation of tracheal
branching
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: 3E5EF7F0-F248-11E8-B48F-1D18A9856A87
volume: 156
year: '2014'
...
---
_id: '9458'
abstract:
- lang: eng
text: Dnmt1 epigenetically propagates symmetrical CG methylation in many eukaryotes.
Their genomes are typically depleted of CG dinucleotides because of imperfect
repair of deaminated methylcytosines. Here, we extensively survey diverse species
lacking Dnmt1 and show that, surprisingly, symmetrical CG methylation is nonetheless
frequently present and catalyzed by a different DNA methyltransferase family,
Dnmt5. Numerous Dnmt5-containing organisms that diverged more than a billion years
ago exhibit clustered methylation, specifically in nucleosome linkers. Clustered
methylation occurs at unprecedented densities and directly disfavors nucleosomes,
contributing to nucleosome positioning between clusters. Dense methylation is
enabled by a regime of genomic sequence evolution that enriches CG dinucleotides
and drives the highest CG frequencies known. Species with linker methylation have
small, transcriptionally active nuclei that approach the physical limits of chromatin
compaction. These features constitute a previously unappreciated genome architecture,
in which dense methylation influences nucleosome positions, likely facilitating
nuclear processes under extreme spatial constraints.
article_processing_charge: No
article_type: original
author:
- first_name: Jason T.
full_name: Huff, Jason T.
last_name: Huff
- first_name: Daniel
full_name: Zilberman, Daniel
id: 6973db13-dd5f-11ea-814e-b3e5455e9ed1
last_name: Zilberman
orcid: 0000-0002-0123-8649
citation:
ama: Huff JT, Zilberman D. Dnmt1-independent CG methylation contributes to nucleosome
positioning in diverse eukaryotes. Cell. 2014;156(6):1286-1297. doi:10.1016/j.cell.2014.01.029
apa: Huff, J. T., & Zilberman, D. (2014). Dnmt1-independent CG methylation contributes
to nucleosome positioning in diverse eukaryotes. Cell. Elsevier. https://doi.org/10.1016/j.cell.2014.01.029
chicago: Huff, Jason T., and Daniel Zilberman. “Dnmt1-Independent CG Methylation
Contributes to Nucleosome Positioning in Diverse Eukaryotes.” Cell. Elsevier,
2014. https://doi.org/10.1016/j.cell.2014.01.029.
ieee: J. T. Huff and D. Zilberman, “Dnmt1-independent CG methylation contributes
to nucleosome positioning in diverse eukaryotes,” Cell, vol. 156, no. 6.
Elsevier, pp. 1286–1297, 2014.
ista: Huff JT, Zilberman D. 2014. Dnmt1-independent CG methylation contributes to
nucleosome positioning in diverse eukaryotes. Cell. 156(6), 1286–1297.
mla: Huff, Jason T., and Daniel Zilberman. “Dnmt1-Independent CG Methylation Contributes
to Nucleosome Positioning in Diverse Eukaryotes.” Cell, vol. 156, no. 6,
Elsevier, 2014, pp. 1286–97, doi:10.1016/j.cell.2014.01.029.
short: J.T. Huff, D. Zilberman, Cell 156 (2014) 1286–1297.
date_created: 2021-06-04T12:00:16Z
date_published: 2014-03-13T00:00:00Z
date_updated: 2021-12-14T08:22:36Z
day: '13'
department:
- _id: DaZi
doi: 10.1016/j.cell.2014.01.029
extern: '1'
external_id:
pmid:
- '24630728'
intvolume: ' 156'
issue: '6'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1016/j.cell.2014.01.029
month: '03'
oa: 1
oa_version: Published Version
page: 1286-1297
pmid: 1
publication: Cell
publication_identifier:
eissn:
- 1097-4172
issn:
- 0092-8674
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: Dnmt1-independent CG methylation contributes to nucleosome positioning in diverse
eukaryotes
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 156
year: '2014'
...
---
_id: '11085'
abstract:
- lang: eng
text: During mitotic exit, missegregated chromosomes can recruit their own nuclear
envelope (NE) to form micronuclei (MN). MN have reduced functioning compared to
primary nuclei in the same cell, although the two compartments appear to be structurally
comparable. Here we show that over 60% of MN undergo an irreversible loss of compartmentalization
during interphase due to NE collapse. This disruption of the MN, which is induced
by defects in nuclear lamina assembly, drastically reduces nuclear functions and
can trigger massive DNA damage. MN disruption is associated with chromatin compaction
and invasion of endoplasmic reticulum (ER) tubules into the chromatin. We identified
disrupted MN in both major subtypes of human non-small-cell lung cancer, suggesting
that disrupted MN could be a useful objective biomarker for genomic instability
in solid tumors. Our study shows that NE collapse is a key event underlying MN
dysfunction and establishes a link between aberrant NE organization and aneuploidy.
article_processing_charge: No
article_type: original
author:
- first_name: Emily M.
full_name: Hatch, Emily M.
last_name: Hatch
- first_name: Andrew H.
full_name: Fischer, Andrew H.
last_name: Fischer
- first_name: Thomas J.
full_name: Deerinck, Thomas J.
last_name: Deerinck
- first_name: Martin W
full_name: HETZER, Martin W
id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed
last_name: HETZER
orcid: 0000-0002-2111-992X
citation:
ama: Hatch EM, Fischer AH, Deerinck TJ, Hetzer M. Catastrophic nuclear envelope
collapse in cancer cell micronuclei. Cell. 2013;154(1):47-60. doi:10.1016/j.cell.2013.06.007
apa: Hatch, E. M., Fischer, A. H., Deerinck, T. J., & Hetzer, M. (2013). Catastrophic
nuclear envelope collapse in cancer cell micronuclei. Cell. Elsevier. https://doi.org/10.1016/j.cell.2013.06.007
chicago: Hatch, Emily M., Andrew H. Fischer, Thomas J. Deerinck, and Martin Hetzer.
“Catastrophic Nuclear Envelope Collapse in Cancer Cell Micronuclei.” Cell.
Elsevier, 2013. https://doi.org/10.1016/j.cell.2013.06.007.
ieee: E. M. Hatch, A. H. Fischer, T. J. Deerinck, and M. Hetzer, “Catastrophic nuclear
envelope collapse in cancer cell micronuclei,” Cell, vol. 154, no. 1. Elsevier,
pp. 47–60, 2013.
ista: Hatch EM, Fischer AH, Deerinck TJ, Hetzer M. 2013. Catastrophic nuclear envelope
collapse in cancer cell micronuclei. Cell. 154(1), 47–60.
mla: Hatch, Emily M., et al. “Catastrophic Nuclear Envelope Collapse in Cancer Cell
Micronuclei.” Cell, vol. 154, no. 1, Elsevier, 2013, pp. 47–60, doi:10.1016/j.cell.2013.06.007.
short: E.M. Hatch, A.H. Fischer, T.J. Deerinck, M. Hetzer, Cell 154 (2013) 47–60.
date_created: 2022-04-07T07:50:51Z
date_published: 2013-07-03T00:00:00Z
date_updated: 2022-07-18T08:45:47Z
day: '03'
doi: 10.1016/j.cell.2013.06.007
extern: '1'
external_id:
pmid:
- '23827674'
intvolume: ' 154'
issue: '1'
keyword:
- General Biochemistry
- Genetics and Molecular Biology
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1016/j.cell.2013.06.007
month: '07'
oa: 1
oa_version: Published Version
page: 47-60
pmid: 1
publication: Cell
publication_identifier:
issn:
- 0092-8674
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: Catastrophic nuclear envelope collapse in cancer cell micronuclei
type: journal_article
user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd
volume: 154
year: '2013'
...
---
_id: '11087'
abstract:
- lang: eng
text: Intracellular proteins with long lifespans have recently been linked to age-dependent
defects, ranging from decreased fertility to the functional decline of neurons.
Why long-lived proteins exist in metabolically active cellular environments and
how they are maintained over time remains poorly understood. Here, we provide
a system-wide identification of proteins with exceptional lifespans in the rat
brain. These proteins are inefficiently replenished despite being translated robustly
throughout adulthood. Using nucleoporins as a paradigm for long-term protein persistence,
we found that nuclear pore complexes (NPCs) are maintained over a cell’s life
through slow but finite exchange of even its most stable subcomplexes. This maintenance
is limited, however, as some nucleoporin levels decrease during aging, providing
a rationale for the previously observed age-dependent deterioration of NPC function.
Our identification of a long-lived proteome reveals cellular components that are
at increased risk for damage accumulation, linking long-term protein persistence
to the cellular aging process.
article_processing_charge: No
article_type: original
author:
- first_name: Brandon H.
full_name: Toyama, Brandon H.
last_name: Toyama
- first_name: Jeffrey N.
full_name: Savas, Jeffrey N.
last_name: Savas
- first_name: Sung Kyu
full_name: Park, Sung Kyu
last_name: Park
- first_name: Michael S.
full_name: Harris, Michael S.
last_name: Harris
- first_name: Nicholas T.
full_name: Ingolia, Nicholas T.
last_name: Ingolia
- first_name: John R.
full_name: Yates, John R.
last_name: Yates
- first_name: Martin W
full_name: HETZER, Martin W
id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed
last_name: HETZER
orcid: 0000-0002-2111-992X
citation:
ama: Toyama BH, Savas JN, Park SK, et al. Identification of long-lived proteins
reveals exceptional stability of essential cellular structures. Cell. 2013;154(5):971-982.
doi:10.1016/j.cell.2013.07.037
apa: Toyama, B. H., Savas, J. N., Park, S. K., Harris, M. S., Ingolia, N. T., Yates,
J. R., & Hetzer, M. (2013). Identification of long-lived proteins reveals
exceptional stability of essential cellular structures. Cell. Elsevier.
https://doi.org/10.1016/j.cell.2013.07.037
chicago: Toyama, Brandon H., Jeffrey N. Savas, Sung Kyu Park, Michael S. Harris,
Nicholas T. Ingolia, John R. Yates, and Martin Hetzer. “Identification of Long-Lived
Proteins Reveals Exceptional Stability of Essential Cellular Structures.” Cell.
Elsevier, 2013. https://doi.org/10.1016/j.cell.2013.07.037.
ieee: B. H. Toyama et al., “Identification of long-lived proteins reveals
exceptional stability of essential cellular structures,” Cell, vol. 154,
no. 5. Elsevier, pp. 971–982, 2013.
ista: Toyama BH, Savas JN, Park SK, Harris MS, Ingolia NT, Yates JR, Hetzer M. 2013.
Identification of long-lived proteins reveals exceptional stability of essential
cellular structures. Cell. 154(5), 971–982.
mla: Toyama, Brandon H., et al. “Identification of Long-Lived Proteins Reveals Exceptional
Stability of Essential Cellular Structures.” Cell, vol. 154, no. 5, Elsevier,
2013, pp. 971–82, doi:10.1016/j.cell.2013.07.037.
short: B.H. Toyama, J.N. Savas, S.K. Park, M.S. Harris, N.T. Ingolia, J.R. Yates,
M. Hetzer, Cell 154 (2013) 971–982.
date_created: 2022-04-07T07:51:08Z
date_published: 2013-08-29T00:00:00Z
date_updated: 2022-07-18T08:50:47Z
day: '29'
doi: 10.1016/j.cell.2013.07.037
extern: '1'
external_id:
pmid:
- '23993091'
intvolume: ' 154'
issue: '5'
keyword:
- General Biochemistry
- Genetics and Molecular Biology
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1016/j.cell.2013.07.037
month: '08'
oa: 1
oa_version: Published Version
page: 971-982
pmid: 1
publication: Cell
publication_identifier:
issn:
- 0092-8674
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: Identification of long-lived proteins reveals exceptional stability of essential
cellular structures
type: journal_article
user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd
volume: 154
year: '2013'
...
---
_id: '9459'
abstract:
- lang: eng
text: Nucleosome remodelers of the DDM1/Lsh family are required for DNA methylation
of transposable elements, but the reason for this is unknown. How DDM1 interacts
with other methylation pathways, such as small-RNA-directed DNA methylation (RdDM),
which is thought to mediate plant asymmetric methylation through DRM enzymes,
is also unclear. Here, we show that most asymmetric methylation is facilitated
by DDM1 and mediated by the methyltransferase CMT2 separately from RdDM. We find
that heterochromatic sequences preferentially require DDM1 for DNA methylation
and that this preference depends on linker histone H1. RdDM is instead inhibited
by heterochromatin and absolutely requires the nucleosome remodeler DRD1. Together,
DDM1 and RdDM mediate nearly all transposon methylation and collaborate to repress
transposition and regulate the methylation and expression of genes. Our results
indicate that DDM1 provides DNA methyltransferases access to H1-containing heterochromatin
to allow stable silencing of transposable elements in cooperation with the RdDM
pathway.
article_processing_charge: No
article_type: original
author:
- first_name: Assaf
full_name: Zemach, Assaf
last_name: Zemach
- first_name: M. Yvonne
full_name: Kim, M. Yvonne
last_name: Kim
- first_name: Ping-Hung
full_name: Hsieh, Ping-Hung
last_name: Hsieh
- first_name: Devin
full_name: Coleman-Derr, Devin
last_name: Coleman-Derr
- first_name: Leor
full_name: Eshed-Williams, Leor
last_name: Eshed-Williams
- first_name: Ka
full_name: Thao, Ka
last_name: Thao
- first_name: Stacey L.
full_name: Harmer, Stacey L.
last_name: Harmer
- first_name: Daniel
full_name: Zilberman, Daniel
id: 6973db13-dd5f-11ea-814e-b3e5455e9ed1
last_name: Zilberman
orcid: 0000-0002-0123-8649
citation:
ama: Zemach A, Kim MY, Hsieh P-H, et al. The Arabidopsis nucleosome remodeler DDM1
allows DNA methyltransferases to access H1-containing heterochromatin. Cell.
2013;153(1):193-205. doi:10.1016/j.cell.2013.02.033
apa: Zemach, A., Kim, M. Y., Hsieh, P.-H., Coleman-Derr, D., Eshed-Williams, L.,
Thao, K., … Zilberman, D. (2013). The Arabidopsis nucleosome remodeler DDM1 allows
DNA methyltransferases to access H1-containing heterochromatin. Cell. Elsevier.
https://doi.org/10.1016/j.cell.2013.02.033
chicago: Zemach, Assaf, M. Yvonne Kim, Ping-Hung Hsieh, Devin Coleman-Derr, Leor
Eshed-Williams, Ka Thao, Stacey L. Harmer, and Daniel Zilberman. “The Arabidopsis
Nucleosome Remodeler DDM1 Allows DNA Methyltransferases to Access H1-Containing
Heterochromatin.” Cell. Elsevier, 2013. https://doi.org/10.1016/j.cell.2013.02.033.
ieee: A. Zemach et al., “The Arabidopsis nucleosome remodeler DDM1 allows
DNA methyltransferases to access H1-containing heterochromatin,” Cell,
vol. 153, no. 1. Elsevier, pp. 193–205, 2013.
ista: Zemach A, Kim MY, Hsieh P-H, Coleman-Derr D, Eshed-Williams L, Thao K, Harmer
SL, Zilberman D. 2013. The Arabidopsis nucleosome remodeler DDM1 allows DNA methyltransferases
to access H1-containing heterochromatin. Cell. 153(1), 193–205.
mla: Zemach, Assaf, et al. “The Arabidopsis Nucleosome Remodeler DDM1 Allows DNA
Methyltransferases to Access H1-Containing Heterochromatin.” Cell, vol.
153, no. 1, Elsevier, 2013, pp. 193–205, doi:10.1016/j.cell.2013.02.033.
short: A. Zemach, M.Y. Kim, P.-H. Hsieh, D. Coleman-Derr, L. Eshed-Williams, K.
Thao, S.L. Harmer, D. Zilberman, Cell 153 (2013) 193–205.
date_created: 2021-06-04T12:23:28Z
date_published: 2013-03-28T00:00:00Z
date_updated: 2021-12-14T08:25:35Z
day: '28'
department:
- _id: DaZi
doi: 10.1016/j.cell.2013.02.033
extern: '1'
external_id:
pmid:
- '23540698'
intvolume: ' 153'
issue: '1'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1016/j.cell.2013.02.033
month: '03'
oa: 1
oa_version: Published Version
page: 193-205
pmid: 1
publication: Cell
publication_identifier:
eissn:
- 1097-4172
issn:
- 0092-8674
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: The Arabidopsis nucleosome remodeler DDM1 allows DNA methyltransferases to
access H1-containing heterochromatin
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 153
year: '2013'
...
---
_id: '11090'
abstract:
- lang: eng
text: Nuclear export of mRNAs is thought to occur exclusively through nuclear pore
complexes. In this issue of Cell, Speese et al. identify an alternate pathway
for mRNA export in muscle cells where ribonucleoprotein complexes involved in
forming neuromuscular junctions transit the nuclear envelope by fusing with and
budding through the nuclear membrane.
article_processing_charge: No
article_type: letter_note
author:
- first_name: Emily M.
full_name: Hatch, Emily M.
last_name: Hatch
- first_name: Martin W
full_name: HETZER, Martin W
id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed
last_name: HETZER
orcid: 0000-0002-2111-992X
citation:
ama: Hatch EM, Hetzer M. RNP export by nuclear envelope budding. Cell. 2012;149(4):733-735.
doi:10.1016/j.cell.2012.04.018
apa: Hatch, E. M., & Hetzer, M. (2012). RNP export by nuclear envelope budding.
Cell. Elsevier. https://doi.org/10.1016/j.cell.2012.04.018
chicago: Hatch, Emily M., and Martin Hetzer. “RNP Export by Nuclear Envelope Budding.”
Cell. Elsevier, 2012. https://doi.org/10.1016/j.cell.2012.04.018.
ieee: E. M. Hatch and M. Hetzer, “RNP export by nuclear envelope budding,” Cell,
vol. 149, no. 4. Elsevier, pp. 733–735, 2012.
ista: Hatch EM, Hetzer M. 2012. RNP export by nuclear envelope budding. Cell. 149(4),
733–735.
mla: Hatch, Emily M., and Martin Hetzer. “RNP Export by Nuclear Envelope Budding.”
Cell, vol. 149, no. 4, Elsevier, 2012, pp. 733–35, doi:10.1016/j.cell.2012.04.018.
short: E.M. Hatch, M. Hetzer, Cell 149 (2012) 733–735.
date_created: 2022-04-07T07:51:45Z
date_published: 2012-05-11T00:00:00Z
date_updated: 2022-07-18T08:58:48Z
day: '11'
doi: 10.1016/j.cell.2012.04.018
extern: '1'
external_id:
pmid:
- '22579277'
intvolume: ' 149'
issue: '4'
keyword:
- General Biochemistry
- Genetics and Molecular Biology
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1016/j.cell.2012.04.018
month: '05'
oa: 1
oa_version: Published Version
page: 733-735
pmid: 1
publication: Cell
publication_identifier:
issn:
- 0092-8674
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: RNP export by nuclear envelope budding
type: journal_article
user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd
volume: 149
year: '2012'
...
---
_id: '11101'
abstract:
- lang: eng
text: In metazoa, nuclear pore complexes (NPCs) assemble from disassembled precursors
into a reforming nuclear envelope (NE) at the end of mitosis and into growing
intact NEs during interphase. Here, we show via RNAi-mediated knockdown that ELYS,
a nucleoporin critical for the recruitment of the essential Nup107/160 complex
to chromatin, is required for NPC assembly at the end of mitosis but not during
interphase. Conversely, the transmembrane nucleoporin POM121 is critical for the
incorporation of the Nup107/160 complex into new assembly sites specifically during
interphase. Strikingly, recruitment of the Nup107/160 complex to an intact NE
involves a membrane curvature-sensing domain of its constituent Nup133, which
is not required for postmitotic NPC formation. Our results suggest that in organisms
with open mitosis, NPCs assemble via two distinct mechanisms to accommodate cell
cycle-dependent differences in NE topology.
article_processing_charge: No
article_type: original
author:
- first_name: Christine M.
full_name: Doucet, Christine M.
last_name: Doucet
- first_name: Jessica A.
full_name: Talamas, Jessica A.
last_name: Talamas
- first_name: Martin W
full_name: HETZER, Martin W
id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed
last_name: HETZER
orcid: 0000-0002-2111-992X
citation:
ama: Doucet CM, Talamas JA, Hetzer M. Cell cycle-dependent differences in nuclear
pore complex assembly in metazoa. Cell. 2010;141(6):1030-1041. doi:10.1016/j.cell.2010.04.036
apa: Doucet, C. M., Talamas, J. A., & Hetzer, M. (2010). Cell cycle-dependent
differences in nuclear pore complex assembly in metazoa. Cell. Elsevier.
https://doi.org/10.1016/j.cell.2010.04.036
chicago: Doucet, Christine M., Jessica A. Talamas, and Martin Hetzer. “Cell Cycle-Dependent
Differences in Nuclear Pore Complex Assembly in Metazoa.” Cell. Elsevier,
2010. https://doi.org/10.1016/j.cell.2010.04.036.
ieee: C. M. Doucet, J. A. Talamas, and M. Hetzer, “Cell cycle-dependent differences
in nuclear pore complex assembly in metazoa,” Cell, vol. 141, no. 6. Elsevier,
pp. 1030–1041, 2010.
ista: Doucet CM, Talamas JA, Hetzer M. 2010. Cell cycle-dependent differences in
nuclear pore complex assembly in metazoa. Cell. 141(6), 1030–1041.
mla: Doucet, Christine M., et al. “Cell Cycle-Dependent Differences in Nuclear Pore
Complex Assembly in Metazoa.” Cell, vol. 141, no. 6, Elsevier, 2010, pp.
1030–41, doi:10.1016/j.cell.2010.04.036.
short: C.M. Doucet, J.A. Talamas, M. Hetzer, Cell 141 (2010) 1030–1041.
date_created: 2022-04-07T07:53:29Z
date_published: 2010-06-11T00:00:00Z
date_updated: 2022-07-18T08:54:52Z
day: '11'
doi: 10.1016/j.cell.2010.04.036
extern: '1'
external_id:
pmid:
- '20550937'
intvolume: ' 141'
issue: '6'
keyword:
- General Biochemistry
- Genetics and Molecular Biology
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1016/j.cell.2010.04.036
month: '06'
oa: 1
oa_version: Published Version
page: 1030-1041
pmid: 1
publication: Cell
publication_identifier:
issn:
- 0092-8674
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: Cell cycle-dependent differences in nuclear pore complex assembly in metazoa
type: journal_article
user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd
volume: 141
year: '2010'
...
---
_id: '11102'
abstract:
- lang: eng
text: Nuclear pore complexes have recently been shown to play roles in gene activation;
however their potential involvement in metazoan transcription remains unclear.
Here we show that the nucleoporins Sec13, Nup98, and Nup88, as well as a group
of FG-repeat nucleoporins, bind to the Drosophila genome at functionally distinct
loci that often do not represent nuclear envelope contact sites. Whereas Nup88
localizes to silent loci, Sec13, Nup98, and a subset of FG-repeat nucleoporins
bind to developmentally regulated genes undergoing transcription induction. Strikingly,
RNAi-mediated knockdown of intranuclear Sec13 and Nup98 specifically inhibits
transcription of their target genes and prevents efficient reactivation of transcription
after heat shock, suggesting an essential role of NPC components in regulating
complex gene expression programs of multicellular organisms.
article_processing_charge: No
article_type: original
author:
- first_name: Maya
full_name: Capelson, Maya
last_name: Capelson
- first_name: Yun
full_name: Liang, Yun
last_name: Liang
- first_name: Roberta
full_name: Schulte, Roberta
last_name: Schulte
- first_name: William
full_name: Mair, William
last_name: Mair
- first_name: Ulrich
full_name: Wagner, Ulrich
last_name: Wagner
- first_name: Martin W
full_name: HETZER, Martin W
id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed
last_name: HETZER
orcid: 0000-0002-2111-992X
citation:
ama: Capelson M, Liang Y, Schulte R, Mair W, Wagner U, Hetzer M. Chromatin-bound
nuclear pore components regulate gene expression in higher eukaryotes. Cell.
2010;140(3):372-383. doi:10.1016/j.cell.2009.12.054
apa: Capelson, M., Liang, Y., Schulte, R., Mair, W., Wagner, U., & Hetzer, M.
(2010). Chromatin-bound nuclear pore components regulate gene expression in higher
eukaryotes. Cell. Elsevier. https://doi.org/10.1016/j.cell.2009.12.054
chicago: Capelson, Maya, Yun Liang, Roberta Schulte, William Mair, Ulrich Wagner,
and Martin Hetzer. “Chromatin-Bound Nuclear Pore Components Regulate Gene Expression
in Higher Eukaryotes.” Cell. Elsevier, 2010. https://doi.org/10.1016/j.cell.2009.12.054.
ieee: M. Capelson, Y. Liang, R. Schulte, W. Mair, U. Wagner, and M. Hetzer, “Chromatin-bound
nuclear pore components regulate gene expression in higher eukaryotes,” Cell,
vol. 140, no. 3. Elsevier, pp. 372–383, 2010.
ista: Capelson M, Liang Y, Schulte R, Mair W, Wagner U, Hetzer M. 2010. Chromatin-bound
nuclear pore components regulate gene expression in higher eukaryotes. Cell. 140(3),
372–383.
mla: Capelson, Maya, et al. “Chromatin-Bound Nuclear Pore Components Regulate Gene
Expression in Higher Eukaryotes.” Cell, vol. 140, no. 3, Elsevier, 2010,
pp. 372–83, doi:10.1016/j.cell.2009.12.054.
short: M. Capelson, Y. Liang, R. Schulte, W. Mair, U. Wagner, M. Hetzer, Cell 140
(2010) 372–383.
date_created: 2022-04-07T07:53:36Z
date_published: 2010-02-05T00:00:00Z
date_updated: 2022-07-18T08:55:03Z
day: '05'
doi: 10.1016/j.cell.2009.12.054
extern: '1'
external_id:
pmid:
- '20144761'
intvolume: ' 140'
issue: '3'
keyword:
- General Biochemistry
- Genetics and Molecular Biology
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1016/j.cell.2009.12.054
month: '02'
oa: 1
oa_version: Published Version
page: 372-383
pmid: 1
publication: Cell
publication_identifier:
issn:
- 0092-8674
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: Chromatin-bound nuclear pore components regulate gene expression in higher
eukaryotes
type: journal_article
user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd
volume: 140
year: '2010'
...
---
_id: '7703'
abstract:
- lang: eng
text: By combining gene expression profiling with image registration, Tomer et al.
(2010) find that the mushroom body of the segmented worm Platynereis dumerilii
shares many features with the mammalian cerebral cortex. The authors propose that
the mushroom body and cortex evolved from the same structure in the common ancestor
of vertebrates and invertebrates.
article_processing_charge: No
article_type: original
author:
- first_name: Lora Beatrice Jaeger
full_name: Sweeney, Lora Beatrice Jaeger
id: 56BE8254-C4F0-11E9-8E45-0B23E6697425
last_name: Sweeney
orcid: 0000-0001-9242-5601
- first_name: Liqun
full_name: Luo, Liqun
last_name: Luo
citation:
ama: 'Sweeney LB, Luo L. ‘Fore brain: A hint of the ancestral cortex. Cell.
2010;142(5):679-681. doi:10.1016/j.cell.2010.08.024'
apa: 'Sweeney, L. B., & Luo, L. (2010). ‘Fore brain: A hint of the ancestral
cortex. Cell. Elsevier. https://doi.org/10.1016/j.cell.2010.08.024'
chicago: 'Sweeney, Lora B., and Liqun Luo. “‘Fore Brain: A Hint of the Ancestral
Cortex.” Cell. Elsevier, 2010. https://doi.org/10.1016/j.cell.2010.08.024.'
ieee: 'L. B. Sweeney and L. Luo, “‘Fore brain: A hint of the ancestral cortex,”
Cell, vol. 142, no. 5. Elsevier, pp. 679–681, 2010.'
ista: 'Sweeney LB, Luo L. 2010. ‘Fore brain: A hint of the ancestral cortex. Cell.
142(5), 679–681.'
mla: 'Sweeney, Lora B., and Liqun Luo. “‘Fore Brain: A Hint of the Ancestral Cortex.”
Cell, vol. 142, no. 5, Elsevier, 2010, pp. 679–81, doi:10.1016/j.cell.2010.08.024.'
short: L.B. Sweeney, L. Luo, Cell 142 (2010) 679–681.
date_created: 2020-04-30T10:36:52Z
date_published: 2010-09-03T00:00:00Z
date_updated: 2024-01-31T10:14:59Z
day: '03'
doi: 10.1016/j.cell.2010.08.024
extern: '1'
intvolume: ' 142'
issue: '5'
language:
- iso: eng
month: '09'
oa_version: None
page: 679-681
publication: Cell
publication_identifier:
issn:
- 0092-8674
publication_status: published
publisher: Elsevier
quality_controlled: '1'
status: public
title: '‘Fore brain: A hint of the ancestral cortex'
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 142
year: '2010'
...
---
_id: '11108'
abstract:
- lang: eng
text: In dividing cells, nuclear pore complexes (NPCs) disassemble during mitosis
and reassemble into the newly forming nuclei. However, the fate of nuclear pores
in postmitotic cells is unknown. Here, we show that NPCs, unlike other nuclear
structures, do not turn over in differentiated cells. While a subset of NPC components,
like Nup153 and Nup50, are continuously exchanged, scaffold nucleoporins, like
the Nup107/160 complex, are extremely long-lived and remain incorporated in the
nuclear membrane during the entire cellular life span. Besides the lack of nucleoporin
expression and NPC turnover, we discovered an age-related deterioration of NPCs,
leading to an increase in nuclear permeability and the leaking of cytoplasmic
proteins into the nucleus. Our finding that nuclear “leakiness” is dramatically
accelerated during aging and that a subset of nucleoporins is oxidatively damaged
in old cells suggests that the accumulation of damage at the NPC might be a crucial
aging event.
article_processing_charge: No
article_type: original
author:
- first_name: Maximiliano A.
full_name: D'Angelo, Maximiliano A.
last_name: D'Angelo
- first_name: Marcela
full_name: Raices, Marcela
last_name: Raices
- first_name: Siler H.
full_name: Panowski, Siler H.
last_name: Panowski
- first_name: Martin W
full_name: HETZER, Martin W
id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed
last_name: HETZER
orcid: 0000-0002-2111-992X
citation:
ama: D’Angelo MA, Raices M, Panowski SH, Hetzer M. Age-dependent deterioration of
nuclear pore complexes causes a loss of nuclear integrity in postmitotic cells.
Cell. 2009;136(2):284-295. doi:10.1016/j.cell.2008.11.037
apa: D’Angelo, M. A., Raices, M., Panowski, S. H., & Hetzer, M. (2009). Age-dependent
deterioration of nuclear pore complexes causes a loss of nuclear integrity in
postmitotic cells. Cell. Elsevier. https://doi.org/10.1016/j.cell.2008.11.037
chicago: D’Angelo, Maximiliano A., Marcela Raices, Siler H. Panowski, and Martin
Hetzer. “Age-Dependent Deterioration of Nuclear Pore Complexes Causes a Loss of
Nuclear Integrity in Postmitotic Cells.” Cell. Elsevier, 2009. https://doi.org/10.1016/j.cell.2008.11.037.
ieee: M. A. D’Angelo, M. Raices, S. H. Panowski, and M. Hetzer, “Age-dependent deterioration
of nuclear pore complexes causes a loss of nuclear integrity in postmitotic cells,”
Cell, vol. 136, no. 2. Elsevier, pp. 284–295, 2009.
ista: D’Angelo MA, Raices M, Panowski SH, Hetzer M. 2009. Age-dependent deterioration
of nuclear pore complexes causes a loss of nuclear integrity in postmitotic cells.
Cell. 136(2), 284–295.
mla: D’Angelo, Maximiliano A., et al. “Age-Dependent Deterioration of Nuclear Pore
Complexes Causes a Loss of Nuclear Integrity in Postmitotic Cells.” Cell,
vol. 136, no. 2, Elsevier, 2009, pp. 284–95, doi:10.1016/j.cell.2008.11.037.
short: M.A. D’Angelo, M. Raices, S.H. Panowski, M. Hetzer, Cell 136 (2009) 284–295.
date_created: 2022-04-07T07:54:52Z
date_published: 2009-01-23T00:00:00Z
date_updated: 2022-07-18T08:55:29Z
day: '23'
doi: 10.1016/j.cell.2008.11.037
extern: '1'
external_id:
pmid:
- '19167330'
intvolume: ' 136'
issue: '2'
keyword:
- General Biochemistry
- Genetics and Molecular Biology
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1016/j.cell.2008.11.037
month: '01'
oa: 1
oa_version: Published Version
page: 284-295
pmid: 1
publication: Cell
publication_identifier:
issn:
- 0092-8674
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: Age-dependent deterioration of nuclear pore complexes causes a loss of nuclear
integrity in postmitotic cells
type: journal_article
user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd
volume: 136
year: '2009'
...
---
_id: '7704'
abstract:
- lang: eng
text: Gradients of axon guidance molecules instruct the formation of continuous
neural maps, such as the retinotopic map in the vertebrate visual system. Here
we show that molecular gradients can also instruct the formation of a discrete
neural map. In the fly olfactory system, axons of 50 classes of olfactory receptor
neurons (ORNs) and dendrites of 50 classes of projection neurons (PNs) form one-to-one
connections at discrete units called glomeruli. We provide expression, loss- and
gain-of-function data to demonstrate that the levels of transmembrane Semaphorin-1a
(Sema-1a), acting cell-autonomously as a receptor or part of a receptor complex,
direct the dendritic targeting of PNs along the dorsolateral to ventromedial axis
of the antennal lobe. Sema-1a also regulates PN axon targeting in higher olfactory
centers. Thus, graded expression of Sema-1a contributes to connection specificity
from ORNs to PNs and then to higher brain centers, ensuring proper representation
of olfactory information in the brain.
article_processing_charge: No
article_type: original
author:
- first_name: Takaki
full_name: Komiyama, Takaki
last_name: Komiyama
- first_name: Lora Beatrice Jaeger
full_name: Sweeney, Lora Beatrice Jaeger
id: 56BE8254-C4F0-11E9-8E45-0B23E6697425
last_name: Sweeney
orcid: 0000-0001-9242-5601
- first_name: Oren
full_name: Schuldiner, Oren
last_name: Schuldiner
- first_name: K. Christopher
full_name: Garcia, K. Christopher
last_name: Garcia
- first_name: Liqun
full_name: Luo, Liqun
last_name: Luo
citation:
ama: Komiyama T, Sweeney LB, Schuldiner O, Garcia KC, Luo L. Graded expression of
semaphorin-1a cell-autonomously directs dendritic targeting of olfactory projection
neurons. Cell. 2007;128(2):399-410. doi:10.1016/j.cell.2006.12.028
apa: Komiyama, T., Sweeney, L. B., Schuldiner, O., Garcia, K. C., & Luo, L.
(2007). Graded expression of semaphorin-1a cell-autonomously directs dendritic
targeting of olfactory projection neurons. Cell. Elsevier. https://doi.org/10.1016/j.cell.2006.12.028
chicago: Komiyama, Takaki, Lora B. Sweeney, Oren Schuldiner, K. Christopher Garcia,
and Liqun Luo. “Graded Expression of Semaphorin-1a Cell-Autonomously Directs Dendritic
Targeting of Olfactory Projection Neurons.” Cell. Elsevier, 2007. https://doi.org/10.1016/j.cell.2006.12.028.
ieee: T. Komiyama, L. B. Sweeney, O. Schuldiner, K. C. Garcia, and L. Luo, “Graded
expression of semaphorin-1a cell-autonomously directs dendritic targeting of olfactory
projection neurons,” Cell, vol. 128, no. 2. Elsevier, pp. 399–410, 2007.
ista: Komiyama T, Sweeney LB, Schuldiner O, Garcia KC, Luo L. 2007. Graded expression
of semaphorin-1a cell-autonomously directs dendritic targeting of olfactory projection
neurons. Cell. 128(2), 399–410.
mla: Komiyama, Takaki, et al. “Graded Expression of Semaphorin-1a Cell-Autonomously
Directs Dendritic Targeting of Olfactory Projection Neurons.” Cell, vol.
128, no. 2, Elsevier, 2007, pp. 399–410, doi:10.1016/j.cell.2006.12.028.
short: T. Komiyama, L.B. Sweeney, O. Schuldiner, K.C. Garcia, L. Luo, Cell 128 (2007)
399–410.
date_created: 2020-04-30T10:37:08Z
date_published: 2007-01-26T00:00:00Z
date_updated: 2024-01-31T10:14:48Z
day: '26'
doi: 10.1016/j.cell.2006.12.028
extern: '1'
intvolume: ' 128'
issue: '2'
language:
- iso: eng
month: '01'
oa_version: None
page: 399-410
publication: Cell
publication_identifier:
issn:
- 0092-8674
publication_status: published
publisher: Elsevier
quality_controlled: '1'
status: public
title: Graded expression of semaphorin-1a cell-autonomously directs dendritic targeting
of olfactory projection neurons
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 128
year: '2007'
...