---
_id: '12291'
abstract:
- lang: eng
text: The phytohormone auxin triggers transcriptional reprogramming through a well-characterized
perception machinery in the nucleus. By contrast, mechanisms that underlie fast
effects of auxin, such as the regulation of ion fluxes, rapid phosphorylation
of proteins or auxin feedback on its transport, remain unclear1,2,3. Whether auxin-binding
protein 1 (ABP1) is an auxin receptor has been a source of debate for decades1,4.
Here we show that a fraction of Arabidopsis thaliana ABP1 is secreted and binds
auxin specifically at an acidic pH that is typical of the apoplast. ABP1 and its
plasma-membrane-localized partner, transmembrane kinase 1 (TMK1), are required
for the auxin-induced ultrafast global phospho-response and for downstream processes
that include the activation of H+-ATPase and accelerated cytoplasmic streaming.
abp1 and tmk mutants cannot establish auxin-transporting channels and show defective
auxin-induced vasculature formation and regeneration. An ABP1(M2X) variant that
lacks the capacity to bind auxin is unable to complement these defects in abp1
mutants. These data indicate that ABP1 is the auxin receptor for TMK1-based cell-surface
signalling, which mediates the global phospho-response and auxin canalization.
acknowledged_ssus:
- _id: Bio
- _id: EM-Fac
- _id: LifeSc
acknowledgement: We acknowledge K. Kubiasová for excellent technical assistance, J.
Neuhold, A. Lehner and A. Sedivy for technical assistance with protein production
and purification at Vienna Biocenter Core Facilities; Creoptix for performing GCI;
and the Bioimaging, Electron Microscopy and Life Science Facilities at ISTA, the
Plant Sciences Core Facility of CEITEC Masaryk University, the Core Facility CELLIM
(MEYS CR, LM2018129 Czech-BioImaging) and J. Sprakel for their assistance. J.F.
is grateful to R. Napier for many insightful suggestions and support. We thank all
past and present members of the Friml group for their support and for other contributions
to this effort to clarify the controversial role of ABP1 over the past seven years.
The project received funding from the European Research Council (ERC) under the
European Union’s Horizon 2020 research and innovation program (grant agreement no.
742985 to J.F. and 833867 to D.W.); the Austrian Science Fund (FWF; P29988 to J.F.);
the Netherlands Organization for Scientific Research (NWO; VICI grant 865.14.001
to D.W. and VENI grant VI.Veni.212.003 to A.K.); the Ministry of Education, Science
and Technological Development of the Republic of Serbia (contract no. 451-03-68/2022-14/200053
to B.D.Ž.); and the MEXT/JSPS KAKENHI to K.T. (20K06685) and T.K. (20H05687 and
20H05910).
article_processing_charge: No
article_type: original
author:
- first_name: Jiří
full_name: Friml, Jiří
id: 4159519E-F248-11E8-B48F-1D18A9856A87
last_name: Friml
orcid: 0000-0002-8302-7596
- first_name: Michelle C
full_name: Gallei, Michelle C
id: 35A03822-F248-11E8-B48F-1D18A9856A87
last_name: Gallei
orcid: 0000-0003-1286-7368
- first_name: Zuzana
full_name: Gelová, Zuzana
id: 0AE74790-0E0B-11E9-ABC7-1ACFE5697425
last_name: Gelová
orcid: 0000-0003-4783-1752
- 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: Ewa
full_name: Mazur, Ewa
last_name: Mazur
- first_name: Aline
full_name: Monzer, Aline
id: 2DB5D88C-D7B3-11E9-B8FD-7907E6697425
last_name: Monzer
- first_name: Lesia
full_name: Rodriguez Solovey, Lesia
id: 3922B506-F248-11E8-B48F-1D18A9856A87
last_name: Rodriguez Solovey
orcid: 0000-0002-7244-7237
- first_name: Mark
full_name: Roosjen, Mark
last_name: Roosjen
- first_name: Inge
full_name: Verstraeten, Inge
id: 362BF7FE-F248-11E8-B48F-1D18A9856A87
last_name: Verstraeten
orcid: 0000-0001-7241-2328
- first_name: Branka D.
full_name: Živanović, Branka D.
last_name: Živanović
- first_name: Minxia
full_name: Zou, Minxia
id: 5c243f41-03f3-11ec-841c-96faf48a7ef9
last_name: Zou
- first_name: Lukas
full_name: Fiedler, Lukas
id: 7c417475-8972-11ed-ae7b-8b674ca26986
last_name: Fiedler
- first_name: Caterina
full_name: Giannini, Caterina
id: e3fdddd5-f6e0-11ea-865d-ca99ee6367f4
last_name: Giannini
- first_name: Peter
full_name: Grones, Peter
last_name: Grones
- first_name: Mónika
full_name: Hrtyan, Mónika
id: 45A71A74-F248-11E8-B48F-1D18A9856A87
last_name: Hrtyan
- first_name: Walter
full_name: Kaufmann, Walter
id: 3F99E422-F248-11E8-B48F-1D18A9856A87
last_name: Kaufmann
orcid: 0000-0001-9735-5315
- first_name: Andre
full_name: Kuhn, Andre
last_name: Kuhn
- first_name: Madhumitha
full_name: Narasimhan, Madhumitha
id: 44BF24D0-F248-11E8-B48F-1D18A9856A87
last_name: Narasimhan
orcid: 0000-0002-8600-0671
- first_name: Marek
full_name: Randuch, Marek
id: 6ac4636d-15b2-11ec-abd3-fb8df79972ae
last_name: Randuch
- first_name: Nikola
full_name: Rýdza, Nikola
last_name: Rýdza
- first_name: Koji
full_name: Takahashi, Koji
last_name: Takahashi
- first_name: Shutang
full_name: Tan, Shutang
id: 2DE75584-F248-11E8-B48F-1D18A9856A87
last_name: Tan
orcid: 0000-0002-0471-8285
- first_name: Anastasiia
full_name: Teplova, Anastasiia
id: e3736151-106c-11ec-b916-c2558e2762c6
last_name: Teplova
- first_name: Toshinori
full_name: Kinoshita, Toshinori
last_name: Kinoshita
- first_name: Dolf
full_name: Weijers, Dolf
last_name: Weijers
- first_name: Hana
full_name: Rakusová, Hana
last_name: Rakusová
citation:
ama: Friml J, Gallei MC, Gelová Z, et al. ABP1–TMK auxin perception for global phosphorylation
and auxin canalization. Nature. 2022;609(7927):575-581. doi:10.1038/s41586-022-05187-x
apa: Friml, J., Gallei, M. C., Gelová, Z., Johnson, A. J., Mazur, E., Monzer, A.,
… Rakusová, H. (2022). ABP1–TMK auxin perception for global phosphorylation and
auxin canalization. Nature. Springer Nature. https://doi.org/10.1038/s41586-022-05187-x
chicago: Friml, Jiří, Michelle C Gallei, Zuzana Gelová, Alexander J Johnson, Ewa
Mazur, Aline Monzer, Lesia Rodriguez Solovey, et al. “ABP1–TMK Auxin Perception
for Global Phosphorylation and Auxin Canalization.” Nature. Springer Nature,
2022. https://doi.org/10.1038/s41586-022-05187-x.
ieee: J. Friml et al., “ABP1–TMK auxin perception for global phosphorylation
and auxin canalization,” Nature, vol. 609, no. 7927. Springer Nature, pp.
575–581, 2022.
ista: Friml J, Gallei MC, Gelová Z, Johnson AJ, Mazur E, Monzer A, Rodriguez Solovey
L, Roosjen M, Verstraeten I, Živanović BD, Zou M, Fiedler L, Giannini C, Grones
P, Hrtyan M, Kaufmann W, Kuhn A, Narasimhan M, Randuch M, Rýdza N, Takahashi K,
Tan S, Teplova A, Kinoshita T, Weijers D, Rakusová H. 2022. ABP1–TMK auxin perception
for global phosphorylation and auxin canalization. Nature. 609(7927), 575–581.
mla: Friml, Jiří, et al. “ABP1–TMK Auxin Perception for Global Phosphorylation and
Auxin Canalization.” Nature, vol. 609, no. 7927, Springer Nature, 2022,
pp. 575–81, doi:10.1038/s41586-022-05187-x.
short: J. Friml, M.C. Gallei, Z. Gelová, A.J. Johnson, E. Mazur, A. Monzer, L. Rodriguez
Solovey, M. Roosjen, I. Verstraeten, B.D. Živanović, M. Zou, L. Fiedler, C. Giannini,
P. Grones, M. Hrtyan, W. Kaufmann, A. Kuhn, M. Narasimhan, M. Randuch, N. Rýdza,
K. Takahashi, S. Tan, A. Teplova, T. Kinoshita, D. Weijers, H. Rakusová, Nature
609 (2022) 575–581.
date_created: 2023-01-16T10:04:48Z
date_published: 2022-09-15T00:00:00Z
date_updated: 2023-11-07T08:16:09Z
day: '15'
ddc:
- '580'
department:
- _id: JiFr
- _id: GradSch
- _id: EvBe
- _id: EM-Fac
doi: 10.1038/s41586-022-05187-x
ec_funded: 1
external_id:
isi:
- '000851357500002'
pmid:
- '36071161'
file:
- access_level: open_access
checksum: a6055c606aefb900bf62ae3e7d15f921
content_type: application/pdf
creator: amally
date_created: 2023-11-02T17:12:37Z
date_updated: 2023-11-02T17:12:37Z
file_id: '14483'
file_name: Friml Nature 2022_merged.pdf
file_size: 79774945
relation: main_file
success: 1
file_date_updated: 2023-11-02T17:12:37Z
has_accepted_license: '1'
intvolume: ' 609'
isi: 1
issue: '7927'
language:
- iso: eng
month: '09'
oa: 1
oa_version: Submitted Version
page: 575-581
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: Nature
publication_identifier:
eissn:
- 1476-4687
issn:
- 0028-0836
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
scopus_import: '1'
status: public
title: ABP1–TMK auxin perception for global phosphorylation and auxin canalization
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 609
year: '2022'
...
---
_id: '10282'
abstract:
- lang: eng
text: Advanced transcriptome sequencing has revealed that the majority of eukaryotic
genes undergo alternative splicing (AS). Nonetheless, little effort has been dedicated
to investigating the functional relevance of particular splicing events, even
those in the key developmental and hormonal regulators. Combining approaches of
genetics, biochemistry and advanced confocal microscopy, we describe the impact
of alternative splicing on the PIN7 gene in the model plant Arabidopsis thaliana.
PIN7 encodes a polarly localized transporter for the phytohormone auxin and produces
two evolutionarily conserved transcripts, PIN7a and PIN7b. PIN7a and PIN7b, differing
in a four amino acid stretch, exhibit almost identical expression patterns and
subcellular localization. We reveal that they are closely associated and mutually
influence each other's mobility within the plasma membrane. Phenotypic complementation
tests indicate that the functional contribution of PIN7b per se is minor, but
it markedly reduces the prominent PIN7a activity, which is required for correct
seedling apical hook formation and auxin-mediated tropic responses. Our results
establish alternative splicing of the PIN family as a conserved, functionally
relevant mechanism, revealing an additional regulatory level of auxin-mediated
plant development.
acknowledgement: We thank Claus Schwechheimer for the pin34 and pin347 seeds, Yuliia
Mironova for technical assistance, Ksenia Timofeyenko and Dmitry Konovalov for help
with the evolutional analysis, Konstantin Kutashev and Siarhei Dabravolski for assistance
with FRET-FLIM, Huibin Han for advice with hypocotyl imaging, Karel Müller for the
initial qRT-PCR on the tobacco cell lines, Stano Pekár for suggestions regarding
the statistical analysis of the morphodynamic measurements, and Jozef Mravec, Dolf
Weijers and Lindy Abas for their comments on the manuscript. This work was supported
by the Czech Science Foundation (projects 16-26428S and 19-23773S to IK, MH and
KRůžička, 19-18917S to JHumpolíčková and 18-26981S to JF), and the Ministry of Education,
Youth and Sports of the Czech Republic (MEYS, CZ.02.1.01/0.0/0.0/16_019/0000738)
to KRůžička and JHejátko. The imaging facilities of the Institute of Experimental
Botany and CEITEC are supported by MEYS (LM2018129 – Czech BioImaging and CZ.02.1.01/0.0/0.0/16_013/0001775).
The authors declare no competing interests.
article_processing_charge: No
article_type: original
author:
- first_name: Ivan
full_name: Kashkan, Ivan
last_name: Kashkan
- first_name: Mónika
full_name: Hrtyan, Mónika
id: 45A71A74-F248-11E8-B48F-1D18A9856A87
last_name: Hrtyan
- first_name: Katarzyna
full_name: Retzer, Katarzyna
last_name: Retzer
- first_name: Jana
full_name: Humpolíčková, Jana
last_name: Humpolíčková
- first_name: Aswathy
full_name: Jayasree, Aswathy
last_name: Jayasree
- first_name: Roberta
full_name: Filepová, Roberta
last_name: Filepová
- first_name: Zuzana
full_name: Vondráková, Zuzana
last_name: Vondráková
- first_name: Sibu
full_name: Simon, Sibu
id: 4542EF9A-F248-11E8-B48F-1D18A9856A87
last_name: Simon
orcid: 0000-0002-1998-6741
- first_name: Debbie
full_name: Rombaut, Debbie
last_name: Rombaut
- first_name: Thomas B.
full_name: Jacobs, Thomas B.
last_name: Jacobs
- first_name: Mikko J.
full_name: Frilander, Mikko J.
last_name: Frilander
- first_name: Jan
full_name: Hejátko, Jan
last_name: Hejátko
- first_name: Jiří
full_name: Friml, Jiří
id: 4159519E-F248-11E8-B48F-1D18A9856A87
last_name: Friml
orcid: 0000-0002-8302-7596
- first_name: Jan
full_name: Petrášek, Jan
last_name: Petrášek
- first_name: Kamil
full_name: Růžička, Kamil
last_name: Růžička
citation:
ama: Kashkan I, Hrtyan M, Retzer K, et al. Mutually opposing activity of PIN7 splicing
isoforms is required for auxin-mediated tropic responses in Arabidopsis thaliana.
New Phytologist. 2021;233:329-343. doi:10.1111/nph.17792
apa: Kashkan, I., Hrtyan, M., Retzer, K., Humpolíčková, J., Jayasree, A., Filepová,
R., … Růžička, K. (2021). Mutually opposing activity of PIN7 splicing isoforms
is required for auxin-mediated tropic responses in Arabidopsis thaliana. New
Phytologist. Wiley. https://doi.org/10.1111/nph.17792
chicago: Kashkan, Ivan, Mónika Hrtyan, Katarzyna Retzer, Jana Humpolíčková, Aswathy
Jayasree, Roberta Filepová, Zuzana Vondráková, et al. “Mutually Opposing Activity
of PIN7 Splicing Isoforms Is Required for Auxin-Mediated Tropic Responses in Arabidopsis
Thaliana.” New Phytologist. Wiley, 2021. https://doi.org/10.1111/nph.17792.
ieee: I. Kashkan et al., “Mutually opposing activity of PIN7 splicing isoforms
is required for auxin-mediated tropic responses in Arabidopsis thaliana,” New
Phytologist, vol. 233. Wiley, pp. 329–343, 2021.
ista: Kashkan I, Hrtyan M, Retzer K, Humpolíčková J, Jayasree A, Filepová R, Vondráková
Z, Simon S, Rombaut D, Jacobs TB, Frilander MJ, Hejátko J, Friml J, Petrášek J,
Růžička K. 2021. Mutually opposing activity of PIN7 splicing isoforms is required
for auxin-mediated tropic responses in Arabidopsis thaliana. New Phytologist.
233, 329–343.
mla: Kashkan, Ivan, et al. “Mutually Opposing Activity of PIN7 Splicing Isoforms
Is Required for Auxin-Mediated Tropic Responses in Arabidopsis Thaliana.” New
Phytologist, vol. 233, Wiley, 2021, pp. 329–43, doi:10.1111/nph.17792.
short: I. Kashkan, M. Hrtyan, K. Retzer, J. Humpolíčková, A. Jayasree, R. Filepová,
Z. Vondráková, S. Simon, D. Rombaut, T.B. Jacobs, M.J. Frilander, J. Hejátko,
J. Friml, J. Petrášek, K. Růžička, New Phytologist 233 (2021) 329–343.
date_created: 2021-11-14T23:01:24Z
date_published: 2021-11-05T00:00:00Z
date_updated: 2023-08-14T11:46:43Z
day: '05'
department:
- _id: JiFr
doi: 10.1111/nph.17792
external_id:
isi:
- '000714678100001'
pmid:
- '34637542'
intvolume: ' 233'
isi: 1
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://www.biorxiv.org/content/10.1101/2020.05.02.074070v2
month: '11'
oa: 1
oa_version: Preprint
page: 329-343
pmid: 1
publication: New Phytologist
publication_identifier:
eissn:
- 1469-8137
issn:
- 0028-646X
publication_status: published
publisher: Wiley
quality_controlled: '1'
scopus_import: '1'
status: public
title: Mutually opposing activity of PIN7 splicing isoforms is required for auxin-mediated
tropic responses in Arabidopsis thaliana
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 233
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: '6104'
abstract:
- lang: eng
text: Abiotic stress poses constant challenges for plant survival and is a serious
problem for global agricultural productivity. On a molecular level, stress conditions
result in elevation of reactive oxygen species (ROS) production causing oxidative
stress associated with oxidation of proteins and nucleic acids as well as impairment
of membrane functions. Adaptation of root growth to ROS accumulation is facilitated
through modification of auxin and cytokinin hormone homeostasis. Here, we report
that in Arabidopsis root meristem, ROS-induced changes of auxin levels correspond
to decreased abundance of PIN auxin efflux carriers at the plasma membrane (PM).
Specifically, increase in H2O2 levels affects PIN2 endocytic recycling. We show
that the PIN2 intracellular trafficking during adaptation to oxidative stress
requires the function of the ADP-ribosylation factor (ARF)-guanine-nucleotide
exchange factor (GEF) BEN1, an actin-associated regulator of the trafficking from
the PM to early endosomes and, presumably, indirectly, trafficking to the vacuoles.
We propose that H2O2 levels affect the actin dynamics thus modulating ARF-GEF-dependent
trafficking of PIN2. This mechanism provides a way how root growth acclimates
to stress and adapts to a changing environment.
article_processing_charge: No
author:
- first_name: Marta
full_name: Zwiewka, Marta
last_name: Zwiewka
- first_name: Agnieszka
full_name: Bielach, Agnieszka
last_name: Bielach
- first_name: Prashanth
full_name: Tamizhselvan, Prashanth
last_name: Tamizhselvan
- first_name: Sharmila
full_name: Madhavan, Sharmila
last_name: Madhavan
- first_name: Eman Elrefaay
full_name: Ryad, Eman Elrefaay
last_name: Ryad
- first_name: Shutang
full_name: Tan, Shutang
id: 2DE75584-F248-11E8-B48F-1D18A9856A87
last_name: Tan
orcid: 0000-0002-0471-8285
- first_name: Mónika
full_name: Hrtyan, Mónika
id: 45A71A74-F248-11E8-B48F-1D18A9856A87
last_name: Hrtyan
- first_name: Petre
full_name: Dobrev, Petre
last_name: Dobrev
- first_name: Radomira
full_name: Vanková, Radomira
last_name: Vanková
- first_name: Jiří
full_name: Friml, Jiří
id: 4159519E-F248-11E8-B48F-1D18A9856A87
last_name: Friml
orcid: 0000-0002-8302-7596
- first_name: Vanesa B.
full_name: Tognetti, Vanesa B.
last_name: Tognetti
citation:
ama: Zwiewka M, Bielach A, Tamizhselvan P, et al. Root adaptation to H2O2-induced
oxidative stress by ARF-GEF BEN1- and cytoskeleton-mediated PIN2 trafficking.
Plant and Cell Physiology. 2019;60(2):255-273. doi:10.1093/pcp/pcz001
apa: Zwiewka, M., Bielach, A., Tamizhselvan, P., Madhavan, S., Ryad, E. E., Tan,
S., … Tognetti, V. B. (2019). Root adaptation to H2O2-induced oxidative stress
by ARF-GEF BEN1- and cytoskeleton-mediated PIN2 trafficking. Plant and Cell
Physiology. Oxford University Press. https://doi.org/10.1093/pcp/pcz001
chicago: Zwiewka, Marta, Agnieszka Bielach, Prashanth Tamizhselvan, Sharmila Madhavan,
Eman Elrefaay Ryad, Shutang Tan, Mónika Hrtyan, et al. “Root Adaptation to H2O2-Induced
Oxidative Stress by ARF-GEF BEN1- and Cytoskeleton-Mediated PIN2 Trafficking.”
Plant and Cell Physiology. Oxford University Press, 2019. https://doi.org/10.1093/pcp/pcz001.
ieee: M. Zwiewka et al., “Root adaptation to H2O2-induced oxidative stress
by ARF-GEF BEN1- and cytoskeleton-mediated PIN2 trafficking,” Plant and Cell
Physiology, vol. 60, no. 2. Oxford University Press, pp. 255–273, 2019.
ista: Zwiewka M, Bielach A, Tamizhselvan P, Madhavan S, Ryad EE, Tan S, Hrtyan M,
Dobrev P, Vanková R, Friml J, Tognetti VB. 2019. Root adaptation to H2O2-induced
oxidative stress by ARF-GEF BEN1- and cytoskeleton-mediated PIN2 trafficking.
Plant and Cell Physiology. 60(2), 255–273.
mla: Zwiewka, Marta, et al. “Root Adaptation to H2O2-Induced Oxidative Stress by
ARF-GEF BEN1- and Cytoskeleton-Mediated PIN2 Trafficking.” Plant and Cell Physiology,
vol. 60, no. 2, Oxford University Press, 2019, pp. 255–73, doi:10.1093/pcp/pcz001.
short: M. Zwiewka, A. Bielach, P. Tamizhselvan, S. Madhavan, E.E. Ryad, S. Tan,
M. Hrtyan, P. Dobrev, R. Vanková, J. Friml, V.B. Tognetti, Plant and Cell Physiology
60 (2019) 255–273.
date_created: 2019-03-17T22:59:14Z
date_published: 2019-02-01T00:00:00Z
date_updated: 2023-08-25T08:05:28Z
day: '01'
department:
- _id: JiFr
doi: 10.1093/pcp/pcz001
external_id:
isi:
- '000459634300002'
pmid:
- '30668780'
intvolume: ' 60'
isi: 1
issue: '2'
language:
- iso: eng
month: '02'
oa_version: None
page: 255-273
pmid: 1
publication: Plant and Cell Physiology
publication_identifier:
eissn:
- 1471-9053
issn:
- 0032-0781
publication_status: published
publisher: Oxford University Press
quality_controlled: '1'
scopus_import: '1'
status: public
title: Root adaptation to H2O2-induced oxidative stress by ARF-GEF BEN1- and cytoskeleton-mediated
PIN2 trafficking
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 60
year: '2019'
...