---
_id: '10719'
abstract:
- lang: eng
text: Auxin, one of the first identified and most widely studied phytohormones,
has been and will remain a hot topic in plant biology. After more than a century
of passionate exploration, the mysteries of its synthesis, transport, signaling,
and metabolism have largely been unlocked. Due to the rapid development of new
technologies, new methods, and new genetic materials, the study of auxin has entered
the fast lane over the past 30 years. Here, we highlight advances in understanding
auxin signaling, including auxin perception, rapid auxin responses, TRANSPORT
INHIBITOR RESPONSE 1 and AUXIN SIGNALING F-boxes (TIR1/AFBs)-mediated transcriptional
and non-transcriptional branches, and the epigenetic regulation of auxin signaling.
We also focus on feedback inhibition mechanisms that prevent the over-amplification
of auxin signals. In addition, we cover the TRANSMEMBRANE KINASEs (TMKs)-mediated
non-canonical signaling, which converges with TIR1/AFBs-mediated transcriptional
regulation to coordinate plant growth and development. The identification of additional
auxin signaling components and their regulation will continue to open new avenues
of research in this field, leading to an increasingly deeper, more comprehensive
understanding of how auxin signals are interpreted at the cellular level to regulate
plant growth and development.
acknowledgement: "This research was financially supported by the National Natural
Science Foundation of China and the Israel Science Foundation (NSFC-ISF; 32061143005),
National Natural Science Foundation of China (32000225), Natural Science Foundation
of Shandong Province (ZR2020QC036), and China Postdoctoral Science Foundation (2020M682165).\r\n"
article_processing_charge: No
article_type: review
author:
- first_name: Z
full_name: Yu, Z
last_name: Yu
- first_name: F
full_name: Zhang, F
last_name: Zhang
- first_name: Jiří
full_name: Friml, Jiří
id: 4159519E-F248-11E8-B48F-1D18A9856A87
last_name: Friml
orcid: 0000-0002-8302-7596
- first_name: Z
full_name: Ding, Z
last_name: Ding
citation:
ama: 'Yu Z, Zhang F, Friml J, Ding Z. Auxin signaling: Research advances over the
past 30 years. Journal of Integrative Plant Biology. 2022;64(2):371-392.
doi:10.1111/jipb.13225'
apa: 'Yu, Z., Zhang, F., Friml, J., & Ding, Z. (2022). Auxin signaling: Research
advances over the past 30 years. Journal of Integrative Plant Biology.
Wiley. https://doi.org/10.1111/jipb.13225'
chicago: 'Yu, Z, F Zhang, Jiří Friml, and Z Ding. “Auxin Signaling: Research Advances
over the Past 30 Years.” Journal of Integrative Plant Biology. Wiley, 2022.
https://doi.org/10.1111/jipb.13225.'
ieee: 'Z. Yu, F. Zhang, J. Friml, and Z. Ding, “Auxin signaling: Research advances
over the past 30 years,” Journal of Integrative Plant Biology, vol. 64,
no. 2. Wiley, pp. 371–392, 2022.'
ista: 'Yu Z, Zhang F, Friml J, Ding Z. 2022. Auxin signaling: Research advances
over the past 30 years. Journal of Integrative Plant Biology. 64(2), 371–392.'
mla: 'Yu, Z., et al. “Auxin Signaling: Research Advances over the Past 30 Years.”
Journal of Integrative Plant Biology, vol. 64, no. 2, Wiley, 2022, pp.
371–92, doi:10.1111/jipb.13225.'
short: Z. Yu, F. Zhang, J. Friml, Z. Ding, Journal of Integrative Plant Biology
64 (2022) 371–392.
date_created: 2022-02-03T09:52:59Z
date_published: 2022-02-01T00:00:00Z
date_updated: 2023-08-02T14:08:30Z
day: '01'
department:
- _id: JiFr
doi: 10.1111/jipb.13225
external_id:
isi:
- '000761281200011'
pmid:
- '35018726'
intvolume: ' 64'
isi: 1
issue: '2'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1111/jipb.13225
month: '02'
oa: 1
oa_version: Published Version
page: 371-392
pmid: 1
publication: Journal of Integrative Plant Biology
publication_identifier:
eissn:
- 1744-7909
issn:
- 1672-9072
publication_status: published
publisher: Wiley
quality_controlled: '1'
scopus_import: '1'
status: public
title: 'Auxin signaling: Research advances over the past 30 years'
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 64
year: '2022'
...
---
_id: '10768'
abstract:
- lang: eng
text: Among the most fascinated properties of the plant hormone auxin is its ability
to promote formation of its own directional transport routes. These gradually
narrowing auxin channels form from the auxin source toward the sink and involve
coordinated, collective polarization of individual cells. Once established, the
channels provide positional information, along which new vascular strands form,
for example, during organogenesis, regeneration, or leave venation. The main prerequisite
of this still mysterious auxin canalization mechanism is a feedback between auxin
signaling and its directional transport. This is manifested by auxin-induced re-arrangements
of polar, subcellular localization of PIN-FORMED (PIN) auxin exporters. Immanent
open questions relate to how position of auxin source and sink as well as tissue
context are sensed and translated into tissue polarization and how cells communicate
to polarize coordinately. Recently, identification of the first molecular players
opens new avenues into molecular studies of this intriguing example of self-organizing
plant development.
acknowledgement: The authors apologize to those researchers whose work was not cited.
In addition, exciting topics such as PIN polarization in context of phyllotaxis,
shoot branching and termination of gravitropic bending, or role of additional auxin
transporters could not have been included owing to lack of space. This work was
supported by the Czech Science Foundation GAČR (GA18-26981S). The authors also acknowledge
the EMBO for supporting J.H. with a long-term fellowship (ALTF217-2021).
article_number: '102174'
article_processing_charge: Yes (via OA deal)
article_type: original
author:
- first_name: Jakub
full_name: Hajny, Jakub
id: 4800CC20-F248-11E8-B48F-1D18A9856A87
last_name: Hajny
orcid: 0000-0003-2140-7195
- first_name: Shutang
full_name: Tan, Shutang
id: 2DE75584-F248-11E8-B48F-1D18A9856A87
last_name: Tan
orcid: 0000-0002-0471-8285
- first_name: Jiří
full_name: Friml, Jiří
id: 4159519E-F248-11E8-B48F-1D18A9856A87
last_name: Friml
orcid: 0000-0002-8302-7596
citation:
ama: 'Hajny J, Tan S, Friml J. Auxin canalization: From speculative models toward
molecular players. Current Opinion in Plant Biology. 2022;65(2). doi:10.1016/j.pbi.2022.102174'
apa: 'Hajny, J., Tan, S., & Friml, J. (2022). Auxin canalization: From speculative
models toward molecular players. Current Opinion in Plant Biology. Elsevier.
https://doi.org/10.1016/j.pbi.2022.102174'
chicago: 'Hajny, Jakub, Shutang Tan, and Jiří Friml. “Auxin Canalization: From Speculative
Models toward Molecular Players.” Current Opinion in Plant Biology. Elsevier,
2022. https://doi.org/10.1016/j.pbi.2022.102174.'
ieee: 'J. Hajny, S. Tan, and J. Friml, “Auxin canalization: From speculative models
toward molecular players,” Current Opinion in Plant Biology, vol. 65, no.
2. Elsevier, 2022.'
ista: 'Hajny J, Tan S, Friml J. 2022. Auxin canalization: From speculative models
toward molecular players. Current Opinion in Plant Biology. 65(2), 102174.'
mla: 'Hajny, Jakub, et al. “Auxin Canalization: From Speculative Models toward Molecular
Players.” Current Opinion in Plant Biology, vol. 65, no. 2, 102174, Elsevier,
2022, doi:10.1016/j.pbi.2022.102174.'
short: J. Hajny, S. Tan, J. Friml, Current Opinion in Plant Biology 65 (2022).
date_created: 2022-02-20T23:01:32Z
date_published: 2022-02-01T00:00:00Z
date_updated: 2023-08-02T14:29:12Z
day: '01'
ddc:
- '580'
department:
- _id: JiFr
doi: 10.1016/j.pbi.2022.102174
external_id:
isi:
- '000758724700004'
pmid:
- '35123880'
file:
- access_level: open_access
checksum: f1ee02b6fb4200934eeb31fa69120885
content_type: application/pdf
creator: dernst
date_created: 2022-03-10T13:34:09Z
date_updated: 2022-03-10T13:34:09Z
file_id: '10844'
file_name: 2022_CurrentOpPlantBiology_Hajny.pdf
file_size: 820322
relation: main_file
success: 1
file_date_updated: 2022-03-10T13:34:09Z
has_accepted_license: '1'
intvolume: ' 65'
isi: 1
issue: '2'
language:
- iso: eng
month: '02'
oa: 1
oa_version: Published Version
pmid: 1
publication: Current Opinion in Plant Biology
publication_identifier:
issn:
- 1369-5266
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: 'Auxin canalization: From speculative models toward molecular players'
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: 65
year: '2022'
...
---
_id: '10841'
abstract:
- lang: eng
text: In eukaryotes, clathrin-coated vesicles (CCVs) facilitate the internalization
of material from the cell surface as well as the movement of cargo in post-Golgi
trafficking pathways. This diversity of functions is partially provided by multiple
monomeric and multimeric clathrin adaptor complexes that provide compartment and
cargo selectivity. The adaptor-protein assembly polypeptide-1 (AP-1) complex operates
as part of the secretory pathway at the trans-Golgi network (TGN), while the AP-2
complex and the TPLATE complex jointly operate at the plasma membrane to execute
clathrin-mediated endocytosis. Key to our further understanding of clathrin-mediated
trafficking in plants will be the comprehensive identification and characterization
of the network of evolutionarily conserved and plant-specific core and accessory
machinery involved in the formation and targeting of CCVs. To facilitate these
studies, we have analyzed the proteome of enriched TGN/early endosome-derived
and endocytic CCVs isolated from dividing and expanding suspension-cultured Arabidopsis
(Arabidopsis thaliana) cells. Tandem mass spectrometry analysis results were validated
by differential chemical labeling experiments to identify proteins co-enriching
with CCVs. Proteins enriched in CCVs included previously characterized CCV components
and cargos such as the vacuolar sorting receptors in addition to conserved and
plant-specific components whose function in clathrin-mediated trafficking has
not been previously defined. Notably, in addition to AP-1 and AP-2, all subunits
of the AP-4 complex, but not AP-3 or AP-5, were found to be in high abundance
in the CCV proteome. The association of AP-4 with suspension-cultured Arabidopsis
CCVs is further supported via additional biochemical data.
acknowledged_ssus:
- _id: EM-Fac
acknowledgement: 'The authors would like to acknowledge the VIB Proteomics Core Facility
(VIB-UGent Center for Medical Biotechnology in Ghent, Belgium) and the Research
Technology Support Facility Proteomics Core (Michigan State University in East Lansing,
Michigan) for sample analysis, as well as the University of Wisconsin Biotechnology
Center Mass Spectrometry Core Facility (Madison, WI) for help with data processing.
Additionally, we are grateful to Sue Weintraub (UT Health San Antonio) and Sydney
Thomas (UW- Madison) for assistance with data analysis. This research was supported
by grants to S.Y.B. from the National Science Foundation (Nos. 1121998 and 1614915)
and a Vilas Associate Award (University of Wisconsin, Madison, Graduate School);
to J.P. from the National Natural Science Foundation of China (Nos. 91754104, 31820103008,
and 31670283); to I.H. from the National Research Foundation of Korea (No. 2019R1A2B5B03099982).
This research was also supported by the Scientific Service Units (SSU) of IST Austria
through resources provided by the Electron microscopy Facility (EMF). A.J. is supported
by funding from the Austrian Science Fund (FWF): I3630B25 to J.F. A.H. is supported
by funding from the National Science Foundation (NSF IOS Nos. 1025837 and 1147032).'
article_processing_charge: No
article_type: original
author:
- first_name: DA
full_name: Dahhan, DA
last_name: Dahhan
- first_name: GD
full_name: Reynolds, GD
last_name: Reynolds
- first_name: JJ
full_name: Cárdenas, JJ
last_name: Cárdenas
- first_name: D
full_name: Eeckhout, D
last_name: Eeckhout
- 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: K
full_name: Yperman, K
last_name: Yperman
- first_name: Walter
full_name: Kaufmann, Walter
id: 3F99E422-F248-11E8-B48F-1D18A9856A87
last_name: Kaufmann
orcid: 0000-0001-9735-5315
- first_name: N
full_name: Vang, N
last_name: Vang
- first_name: X
full_name: Yan, X
last_name: Yan
- first_name: I
full_name: Hwang, I
last_name: Hwang
- first_name: A
full_name: Heese, A
last_name: Heese
- first_name: G
full_name: De Jaeger, G
last_name: De Jaeger
- first_name: Jiří
full_name: Friml, Jiří
id: 4159519E-F248-11E8-B48F-1D18A9856A87
last_name: Friml
orcid: 0000-0002-8302-7596
- first_name: D
full_name: Van Damme, D
last_name: Van Damme
- first_name: J
full_name: Pan, J
last_name: Pan
- first_name: SY
full_name: Bednarek, SY
last_name: Bednarek
citation:
ama: Dahhan D, Reynolds G, Cárdenas J, et al. Proteomic characterization of isolated
Arabidopsis clathrin-coated vesicles reveals evolutionarily conserved and plant-specific
components. Plant Cell. 2022;34(6):2150-2173. doi:10.1093/plcell/koac071
apa: Dahhan, D., Reynolds, G., Cárdenas, J., Eeckhout, D., Johnson, A. J., Yperman,
K., … Bednarek, S. (2022). Proteomic characterization of isolated Arabidopsis
clathrin-coated vesicles reveals evolutionarily conserved and plant-specific components.
Plant Cell. Oxford Academic. https://doi.org/10.1093/plcell/koac071
chicago: Dahhan, DA, GD Reynolds, JJ Cárdenas, D Eeckhout, Alexander J Johnson,
K Yperman, Walter Kaufmann, et al. “Proteomic Characterization of Isolated Arabidopsis
Clathrin-Coated Vesicles Reveals Evolutionarily Conserved and Plant-Specific Components.”
Plant Cell. Oxford Academic, 2022. https://doi.org/10.1093/plcell/koac071.
ieee: D. Dahhan et al., “Proteomic characterization of isolated Arabidopsis
clathrin-coated vesicles reveals evolutionarily conserved and plant-specific components,”
Plant Cell, vol. 34, no. 6. Oxford Academic, pp. 2150–2173, 2022.
ista: Dahhan D, Reynolds G, Cárdenas J, Eeckhout D, Johnson AJ, Yperman K, Kaufmann
W, Vang N, Yan X, Hwang I, Heese A, De Jaeger G, Friml J, Van Damme D, Pan J,
Bednarek S. 2022. Proteomic characterization of isolated Arabidopsis clathrin-coated
vesicles reveals evolutionarily conserved and plant-specific components. Plant
Cell. 34(6), 2150–2173.
mla: Dahhan, DA, et al. “Proteomic Characterization of Isolated Arabidopsis Clathrin-Coated
Vesicles Reveals Evolutionarily Conserved and Plant-Specific Components.” Plant
Cell, vol. 34, no. 6, Oxford Academic, 2022, pp. 2150–73, doi:10.1093/plcell/koac071.
short: D. Dahhan, G. Reynolds, J. Cárdenas, D. Eeckhout, A.J. Johnson, K. Yperman,
W. Kaufmann, N. Vang, X. Yan, I. Hwang, A. Heese, G. De Jaeger, J. Friml, D. Van
Damme, J. Pan, S. Bednarek, Plant Cell 34 (2022) 2150–2173.
date_created: 2022-03-08T13:47:51Z
date_published: 2022-06-01T00:00:00Z
date_updated: 2023-08-02T14:46:48Z
day: '01'
department:
- _id: JiFr
- _id: EM-Fac
doi: 10.1093/plcell/koac071
external_id:
isi:
- '000767438800001'
pmid:
- '35218346'
intvolume: ' 34'
isi: 1
issue: '6'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1101/2021.09.16.460678
month: '06'
oa: 1
oa_version: Preprint
page: 2150-2173
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: Plant Cell
publication_identifier:
eissn:
- 1532-298x
issn:
- 1040-4651
publication_status: published
publisher: Oxford Academic
quality_controlled: '1'
scopus_import: '1'
status: public
title: Proteomic characterization of isolated Arabidopsis clathrin-coated vesicles
reveals evolutionarily conserved and plant-specific components
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 34
year: '2022'
...
---
_id: '10888'
abstract:
- lang: eng
text: Despite the growing interest in using chemical genetics in plant research,
small molecule target identification remains a major challenge. The cellular thermal
shift assay coupled with high-resolution mass spectrometry (CETSA MS) that monitors
changes in the thermal stability of proteins caused by their interactions with
small molecules, other proteins, or posttranslational modifications, allows the
discovery of drug targets or the study of protein–metabolite and protein–protein
interactions mainly in mammalian cells. To showcase the applicability of this
method in plants, we applied CETSA MS to intact Arabidopsis thaliana cells and
identified the thermal proteome of the plant-specific glycogen synthase kinase
3 (GSK3) inhibitor, bikinin. A comparison between the thermal and the phosphoproteomes
of bikinin revealed the auxin efflux carrier PIN-FORMED1 (PIN1) as a substrate
of the Arabidopsis GSK3s that negatively regulate the brassinosteroid signaling.
We established that PIN1 phosphorylation by the GSK3s is essential for maintaining
its intracellular polarity that is required for auxin-mediated regulation of vascular
patterning in the leaf, thus revealing cross-talk between brassinosteroid and
auxin signaling.
acknowledgement: "We thank Yanhai Yin for providing the anti-BES1 antibody, Johan
Winne and Brenda Callebaut for synthesizing bikinin, Yuki Kondo and Hiroo Fukuda
for published materials, Tomasz Nodzy\x03nski for useful advice, and Martine De
Cock for help in preparing the manuscript. This\r\nwork was supported by the China
Scholarship Council for predoctoral (Q.L. and X.X.) and postdoctoral (Y.Z.) fellowships;
the Agency for Innovation by Science and Technology for a predoctoral fellowship
(W.D.); the Research Foundation-Flanders, Projects G009018N and G002121N (E.R.);
and the VIB TechWatch Fund (E.R.)."
article_number: e2118220119
article_processing_charge: No
article_type: original
author:
- first_name: Qing
full_name: Lu, Qing
last_name: Lu
- first_name: Yonghong
full_name: Zhang, Yonghong
last_name: Zhang
- first_name: Joakim
full_name: Hellner, Joakim
last_name: Hellner
- first_name: Caterina
full_name: Giannini, Caterina
id: e3fdddd5-f6e0-11ea-865d-ca99ee6367f4
last_name: Giannini
- first_name: Xiangyu
full_name: Xu, Xiangyu
last_name: Xu
- first_name: Jarne
full_name: Pauwels, Jarne
last_name: Pauwels
- first_name: Qian
full_name: Ma, Qian
last_name: Ma
- first_name: Wim
full_name: Dejonghe, Wim
last_name: Dejonghe
- first_name: Huibin
full_name: Han, Huibin
id: 31435098-F248-11E8-B48F-1D18A9856A87
last_name: Han
- first_name: Brigitte
full_name: Van De Cotte, Brigitte
last_name: Van De Cotte
- first_name: Francis
full_name: Impens, Francis
last_name: Impens
- first_name: Kris
full_name: Gevaert, Kris
last_name: Gevaert
- first_name: Ive
full_name: De Smet, Ive
last_name: De Smet
- first_name: Jiří
full_name: Friml, Jiří
id: 4159519E-F248-11E8-B48F-1D18A9856A87
last_name: Friml
orcid: 0000-0002-8302-7596
- first_name: Daniel Martinez
full_name: Molina, Daniel Martinez
last_name: Molina
- first_name: Eugenia
full_name: Russinova, Eugenia
last_name: Russinova
citation:
ama: Lu Q, Zhang Y, Hellner J, et al. Proteome-wide cellular thermal shift assay
reveals unexpected cross-talk between brassinosteroid and auxin signaling. Proceedings
of the National Academy of Sciences of the United States of America. 2022;119(11).
doi:10.1073/pnas.2118220119
apa: Lu, Q., Zhang, Y., Hellner, J., Giannini, C., Xu, X., Pauwels, J., … Russinova,
E. (2022). Proteome-wide cellular thermal shift assay reveals unexpected cross-talk
between brassinosteroid and auxin signaling. Proceedings of the National Academy
of Sciences of the United States of America. Proceedings of the National Academy
of Sciences. https://doi.org/10.1073/pnas.2118220119
chicago: Lu, Qing, Yonghong Zhang, Joakim Hellner, Caterina Giannini, Xiangyu Xu,
Jarne Pauwels, Qian Ma, et al. “Proteome-Wide Cellular Thermal Shift Assay Reveals Unexpected
Cross-Talk between Brassinosteroid and Auxin Signaling.” Proceedings of the
National Academy of Sciences of the United States of America. Proceedings
of the National Academy of Sciences, 2022. https://doi.org/10.1073/pnas.2118220119.
ieee: Q. Lu et al., “Proteome-wide cellular thermal shift assay reveals unexpected
cross-talk between brassinosteroid and auxin signaling,” Proceedings of the
National Academy of Sciences of the United States of America, vol. 119, no.
11. Proceedings of the National Academy of Sciences, 2022.
ista: Lu Q, Zhang Y, Hellner J, Giannini C, Xu X, Pauwels J, Ma Q, Dejonghe W, Han
H, Van De Cotte B, Impens F, Gevaert K, De Smet I, Friml J, Molina DM, Russinova
E. 2022. Proteome-wide cellular thermal shift assay reveals unexpected cross-talk
between brassinosteroid and auxin signaling. Proceedings of the National Academy
of Sciences of the United States of America. 119(11), e2118220119.
mla: Lu, Qing, et al. “Proteome-Wide Cellular Thermal Shift Assay Reveals Unexpected
Cross-Talk between Brassinosteroid and Auxin Signaling.” Proceedings of the
National Academy of Sciences of the United States of America, vol. 119, no.
11, e2118220119, Proceedings of the National Academy of Sciences, 2022, doi:10.1073/pnas.2118220119.
short: Q. Lu, Y. Zhang, J. Hellner, C. Giannini, X. Xu, J. Pauwels, Q. Ma, W. Dejonghe,
H. Han, B. Van De Cotte, F. Impens, K. Gevaert, I. De Smet, J. Friml, D.M. Molina,
E. Russinova, Proceedings of the National Academy of Sciences of the United States
of America 119 (2022).
date_created: 2022-03-20T23:01:39Z
date_published: 2022-03-07T00:00:00Z
date_updated: 2023-08-03T06:06:27Z
day: '07'
ddc:
- '580'
department:
- _id: JiFr
doi: 10.1073/pnas.2118220119
external_id:
isi:
- '000771756300008'
pmid:
- '35254915'
file:
- access_level: open_access
checksum: 83e0fea7919570d0b519b41193342571
content_type: application/pdf
creator: dernst
date_created: 2022-03-21T09:19:47Z
date_updated: 2022-03-21T09:19:47Z
file_id: '10910'
file_name: 2022_PNAS_Lu.pdf
file_size: 2169534
relation: main_file
success: 1
file_date_updated: 2022-03-21T09:19:47Z
has_accepted_license: '1'
intvolume: ' 119'
isi: 1
issue: '11'
language:
- iso: eng
license: https://creativecommons.org/licenses/by-nc-nd/4.0/
month: '03'
oa: 1
oa_version: Published Version
pmid: 1
publication: Proceedings of the National Academy of Sciences of the United States
of America
publication_identifier:
eissn:
- 1091-6490
publication_status: published
publisher: Proceedings of the National Academy of Sciences
quality_controlled: '1'
scopus_import: '1'
status: public
title: Proteome-wide cellular thermal shift assay reveals unexpected cross-talk between
brassinosteroid and auxin signaling
tmp:
image: /images/cc_by_nc_nd.png
legal_code_url: https://creativecommons.org/licenses/by-nc-nd/4.0/legalcode
name: Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International
(CC BY-NC-ND 4.0)
short: CC BY-NC-ND (4.0)
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 119
year: '2022'
...
---
_id: '11589'
abstract:
- lang: eng
text: Calcium-dependent protein kinases (CPK) are key components of a wide array
of signaling pathways, translating stress and nutrient signaling into the modulation
of cellular processes such as ion transport and transcription. However, not much
is known about CPKs in endomembrane trafficking. Here, we screened for CPKs that
impact on root growth and gravitropism, by overexpressing constitutively active
forms of CPKs under the control of an inducible promoter in Arabidopsis thaliana.
We found that inducible overexpression of an constitutive active CPK30 (CA-CPK30)
resulted in a loss of root gravitropism and ectopic auxin accumulation in the
root tip. Immunolocalization revealed that CA-CPK30 roots have reduced PIN protein
levels, PIN1 polarity defects and impaired Brefeldin A (BFA)-sensitive trafficking.
Moreover, FM4-64 uptake was reduced, indicative of a defect in endocytosis. The
effects on BFA-sensitive trafficking were not specific to PINs, as BFA could not
induce aggregation of ARF1- and CHC-labeled endosomes in CA-CPK30. Interestingly,
the interference with BFA-body formation, could be reverted by increasing the
extracellular pH, indicating a pH-dependence of this CA-CPK30 effect. Altogether,
our data reveal an important role for CPK30 in root growth regulation and endomembrane
trafficking in Arabidopsis thaliana.
acknowledgement: "RW and JC predoctoral fellows that were supported by the Chinese
Science Counsil. The IPS2 benefits from the support of the LabEx Saclay Plant Sciences-SPS
(ANR-10-LABX-0040-SPS).\r\nWe thank Jen Sheen for establishing and generously sharing
the CKP family clone sets, and for providing useful feedback on the manuscript."
article_number: '862398'
article_processing_charge: No
article_type: original
author:
- first_name: Ren
full_name: Wang, Ren
last_name: Wang
- first_name: Ellie
full_name: Himschoot, Ellie
last_name: Himschoot
- first_name: Jian
full_name: Chen, Jian
last_name: Chen
- first_name: Marie
full_name: Boudsocq, Marie
last_name: Boudsocq
- first_name: Danny
full_name: Geelen, Danny
last_name: Geelen
- first_name: Jiří
full_name: Friml, Jiří
id: 4159519E-F248-11E8-B48F-1D18A9856A87
last_name: Friml
orcid: 0000-0002-8302-7596
- first_name: Tom
full_name: Beeckman, Tom
last_name: Beeckman
- first_name: Steffen
full_name: Vanneste, Steffen
last_name: Vanneste
citation:
ama: Wang R, Himschoot E, Chen J, et al. Constitutive active CPK30 interferes with
root growth and endomembrane trafficking in Arabidopsis thaliana. Frontiers
in Plant Science. 2022;13. doi:10.3389/fpls.2022.862398
apa: Wang, R., Himschoot, E., Chen, J., Boudsocq, M., Geelen, D., Friml, J., … Vanneste,
S. (2022). Constitutive active CPK30 interferes with root growth and endomembrane
trafficking in Arabidopsis thaliana. Frontiers in Plant Science. Frontiers.
https://doi.org/10.3389/fpls.2022.862398
chicago: Wang, Ren, Ellie Himschoot, Jian Chen, Marie Boudsocq, Danny Geelen, Jiří
Friml, Tom Beeckman, and Steffen Vanneste. “Constitutive Active CPK30 Interferes
with Root Growth and Endomembrane Trafficking in Arabidopsis Thaliana.” Frontiers
in Plant Science. Frontiers, 2022. https://doi.org/10.3389/fpls.2022.862398.
ieee: R. Wang et al., “Constitutive active CPK30 interferes with root growth
and endomembrane trafficking in Arabidopsis thaliana,” Frontiers in Plant Science,
vol. 13. Frontiers, 2022.
ista: Wang R, Himschoot E, Chen J, Boudsocq M, Geelen D, Friml J, Beeckman T, Vanneste
S. 2022. Constitutive active CPK30 interferes with root growth and endomembrane
trafficking in Arabidopsis thaliana. Frontiers in Plant Science. 13, 862398.
mla: Wang, Ren, et al. “Constitutive Active CPK30 Interferes with Root Growth and
Endomembrane Trafficking in Arabidopsis Thaliana.” Frontiers in Plant Science,
vol. 13, 862398, Frontiers, 2022, doi:10.3389/fpls.2022.862398.
short: R. Wang, E. Himschoot, J. Chen, M. Boudsocq, D. Geelen, J. Friml, T. Beeckman,
S. Vanneste, Frontiers in Plant Science 13 (2022).
date_created: 2022-07-17T22:01:54Z
date_published: 2022-06-16T00:00:00Z
date_updated: 2023-08-03T12:01:47Z
day: '16'
ddc:
- '580'
department:
- _id: JiFr
doi: 10.3389/fpls.2022.862398
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title: Constitutive active CPK30 interferes with root growth and endomembrane trafficking
in Arabidopsis thaliana
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