---
_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: '10326'
abstract:
- lang: eng
text: Strigolactones (SLs) are carotenoid-derived plant hormones that control shoot
branching and communications between host plants and symbiotic fungi or root parasitic
plants. Extensive studies have identified the key components participating in
SL biosynthesis and signalling, whereas the catabolism or deactivation of endogenous
SLs in planta remains largely unknown. Here, we report that the Arabidopsis carboxylesterase
15 (AtCXE15) and its orthologues function as efficient hydrolases of SLs. We show
that overexpression of AtCXE15 promotes shoot branching by dampening SL-inhibited
axillary bud outgrowth. We further demonstrate that AtCXE15 could bind and efficiently
hydrolyse SLs both in vitro and in planta. We also provide evidence that AtCXE15
is capable of catalysing hydrolysis of diverse SL analogues and that such CXE15-dependent
catabolism of SLs is evolutionarily conserved in seed plants. These results disclose
a catalytic mechanism underlying homoeostatic regulation of SLs in plants, which
also provides a rational approach to spatial-temporally manipulate the endogenous
SLs and thus architecture of crops and ornamental plants.
acknowledgement: We thank J. Li (Institute of Genetics and Developmental Biology,
China) for providing the at14-1, atmax2-1, atmax3-9, atmax4-1, atmax1-1, kai2-2
(Col-0 background) mutants and B. Xu for providing the complementary DNA of P. patens.
We are grateful to L. Wang for assistance with MST, B. Han for assistance with UPLC–MS,
J. Li for assistance with confocal microscopy and B. Mikael and J. Zhang for their
comments on the manuscript. This work was supported by grants from Strategic Priority
Research Program of Chinese Academy of Sciences (Y.H., XDB27030102) and the National
Natural Science Foundation of China (E.X., 31700253; Y.H., 31830055).
article_processing_charge: No
article_type: original
author:
- first_name: Enjun
full_name: Xu, Enjun
last_name: Xu
- first_name: Liang
full_name: Chai, Liang
last_name: Chai
- first_name: Shiqi
full_name: Zhang, Shiqi
last_name: Zhang
- first_name: Ruixue
full_name: Yu, Ruixue
last_name: Yu
- first_name: Xixi
full_name: Zhang, Xixi
id: 61A66458-47E9-11EA-85BA-8AEAAF14E49A
last_name: Zhang
orcid: 0000-0001-7048-4627
- first_name: Chongyi
full_name: Xu, Chongyi
last_name: Xu
- first_name: Yuxin
full_name: Hu, Yuxin
last_name: Hu
citation:
ama: Xu E, Chai L, Zhang S, et al. Catabolism of strigolactones by a carboxylesterase.
Nature Plants. 2021;7:1495–1504. doi:10.1038/s41477-021-01011-y
apa: Xu, E., Chai, L., Zhang, S., Yu, R., Zhang, X., Xu, C., & Hu, Y. (2021).
Catabolism of strigolactones by a carboxylesterase. Nature Plants. Springer
Nature. https://doi.org/10.1038/s41477-021-01011-y
chicago: Xu, Enjun, Liang Chai, Shiqi Zhang, Ruixue Yu, Xixi Zhang, Chongyi Xu,
and Yuxin Hu. “Catabolism of Strigolactones by a Carboxylesterase.” Nature
Plants. Springer Nature, 2021. https://doi.org/10.1038/s41477-021-01011-y.
ieee: E. Xu et al., “Catabolism of strigolactones by a carboxylesterase,”
Nature Plants, vol. 7. Springer Nature, pp. 1495–1504, 2021.
ista: Xu E, Chai L, Zhang S, Yu R, Zhang X, Xu C, Hu Y. 2021. Catabolism of strigolactones
by a carboxylesterase. Nature Plants. 7, 1495–1504.
mla: Xu, Enjun, et al. “Catabolism of Strigolactones by a Carboxylesterase.” Nature
Plants, vol. 7, Springer Nature, 2021, pp. 1495–1504, doi:10.1038/s41477-021-01011-y.
short: E. Xu, L. Chai, S. Zhang, R. Yu, X. Zhang, C. Xu, Y. Hu, Nature Plants 7
(2021) 1495–1504.
date_created: 2021-11-21T23:01:30Z
date_published: 2021-11-11T00:00:00Z
date_updated: 2023-08-14T11:54:02Z
day: '11'
department:
- _id: JiFr
doi: 10.1038/s41477-021-01011-y
external_id:
isi:
- '000717408000002'
pmid:
- '34764442'
intvolume: ' 7'
isi: 1
language:
- iso: eng
month: '11'
oa_version: None
page: '1495–1504 '
pmid: 1
publication: Nature Plants
publication_identifier:
eissn:
- 2055-0278
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
scopus_import: '1'
status: public
title: Catabolism of strigolactones by a carboxylesterase
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 7
year: '2021'
...
---
_id: '9368'
abstract:
- lang: eng
text: The quality control system for messenger RNA (mRNA) is fundamental for cellular
activities in eukaryotes. To elucidate the molecular mechanism of 3'-Phosphoinositide-Dependent
Protein Kinase1 (PDK1), a master regulator that is essential throughout eukaryotic
growth and development, we employed a forward genetic approach to screen for suppressors
of the loss-of-function T-DNA insertion double mutant pdk1.1 pdk1.2 in Arabidopsis
thaliana. Notably, the severe growth attenuation of pdk1.1 pdk1.2 was rescued
by sop21 (suppressor of pdk1.1 pdk1.2), which harbours a loss-of-function mutation
in PELOTA1 (PEL1). PEL1 is a homologue of mammalian PELOTA and yeast (Saccharomyces
cerevisiae) DOM34p, which each form a heterodimeric complex with the GTPase HBS1
(HSP70 SUBFAMILY B SUPPRESSOR1, also called SUPERKILLER PROTEIN7, SKI7), a protein
that is responsible for ribosomal rescue and thereby assures the quality and fidelity
of mRNA molecules during translation. Genetic analysis further revealed that a
dysfunctional PEL1-HBS1 complex failed to degrade the T-DNA-disrupted PDK1 transcripts,
which were truncated but functional, and thus rescued the growth and developmental
defects of pdk1.1 pdk1.2. Our studies demonstrated the functionality of a homologous
PELOTA-HBS1 complex and identified its essential regulatory role in plants, providing
insights into the mechanism of mRNA quality control.
acknowledgement: 'We gratefully acknowledge the Arabidopsis Biological Resource Centre
(ABRC) for providing T-DNA insertional mutants, and Prof. Remko Offringa for sharing
published seeds. We thank Yuchuan Liu (Shanghai OE Biotech Co., Ltd) for help with
proteomics data analysis, Xixi Zhang (IST Austria) for providing the pDONR-P4P1r-mCherry
plasmid, and Yao Xiao (Technical University of Munich), Alexander Johnson (IST Austria)
and Hana Semeradova (IST Austria) for helpful discussions. The study was supported
by National Natural Science Foundation of China (NSFC, 31721001, 91954206, to H.-W.
X.), “Ten-Thousand Talent Program” (to H.-W. X.) and Collaborative Innovation Center
of Crop Stress Biology, Henan Province, and Austrian Science Fund (FWF): I 3630-B25
(to J. F.). S.T. was funded by a European Molecular Biology Organization (EMBO)
long-term postdoctoral fellowship (ALTF 723-2015).'
article_processing_charge: No
article_type: original
author:
- first_name: W
full_name: Kong, W
last_name: Kong
- first_name: Shutang
full_name: Tan, Shutang
id: 2DE75584-F248-11E8-B48F-1D18A9856A87
last_name: Tan
orcid: 0000-0002-0471-8285
- first_name: Q
full_name: Zhao, Q
last_name: Zhao
- first_name: DL
full_name: Lin, DL
last_name: Lin
- first_name: ZH
full_name: Xu, ZH
last_name: Xu
- first_name: Jiří
full_name: Friml, Jiří
id: 4159519E-F248-11E8-B48F-1D18A9856A87
last_name: Friml
orcid: 0000-0002-8302-7596
- first_name: HW
full_name: Xue, HW
last_name: Xue
citation:
ama: Kong W, Tan S, Zhao Q, et al. mRNA surveillance complex PELOTA-HBS1 eegulates
phosphoinositide-sependent protein kinase1 and plant growth. Plant Physiology.
2021;186(4):2003-2020. doi:10.1093/plphys/kiab199
apa: Kong, W., Tan, S., Zhao, Q., Lin, D., Xu, Z., Friml, J., & Xue, H. (2021).
mRNA surveillance complex PELOTA-HBS1 eegulates phosphoinositide-sependent protein
kinase1 and plant growth. Plant Physiology. American Society of Plant Biologists.
https://doi.org/10.1093/plphys/kiab199
chicago: Kong, W, Shutang Tan, Q Zhao, DL Lin, ZH Xu, Jiří Friml, and HW Xue. “MRNA
Surveillance Complex PELOTA-HBS1 Eegulates Phosphoinositide-Sependent Protein
Kinase1 and Plant Growth.” Plant Physiology. American Society of Plant
Biologists, 2021. https://doi.org/10.1093/plphys/kiab199.
ieee: W. Kong et al., “mRNA surveillance complex PELOTA-HBS1 eegulates phosphoinositide-sependent
protein kinase1 and plant growth,” Plant Physiology, vol. 186, no. 4. American
Society of Plant Biologists, pp. 2003–2020, 2021.
ista: Kong W, Tan S, Zhao Q, Lin D, Xu Z, Friml J, Xue H. 2021. mRNA surveillance
complex PELOTA-HBS1 eegulates phosphoinositide-sependent protein kinase1 and plant
growth. Plant Physiology. 186(4), 2003–2020.
mla: Kong, W., et al. “MRNA Surveillance Complex PELOTA-HBS1 Eegulates Phosphoinositide-Sependent
Protein Kinase1 and Plant Growth.” Plant Physiology, vol. 186, no. 4, American
Society of Plant Biologists, 2021, pp. 2003–20, doi:10.1093/plphys/kiab199.
short: W. Kong, S. Tan, Q. Zhao, D. Lin, Z. Xu, J. Friml, H. Xue, Plant Physiology
186 (2021) 2003–2020.
date_created: 2021-05-03T13:28:20Z
date_published: 2021-04-30T00:00:00Z
date_updated: 2023-09-05T12:20:27Z
day: '30'
department:
- _id: JiFr
doi: 10.1093/plphys/kiab199
external_id:
isi:
- '000703922000025'
pmid:
- '33930167'
intvolume: ' 186'
isi: 1
issue: '4'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1093/plphys/kiab199
month: '04'
oa: 1
oa_version: Published Version
page: 2003-2020
pmid: 1
project:
- _id: 256FEF10-B435-11E9-9278-68D0E5697425
grant_number: 723-2015
name: Long Term Fellowship
- _id: 26538374-B435-11E9-9278-68D0E5697425
call_identifier: FWF
grant_number: I03630
name: Molecular mechanisms of endocytic cargo recognition in plants
publication: Plant Physiology
publication_identifier:
eissn:
- 1532-2548
issn:
- 0032-0889
publication_status: published
publisher: American Society of Plant Biologists
quality_controlled: '1'
status: public
title: mRNA surveillance complex PELOTA-HBS1 eegulates phosphoinositide-sependent
protein kinase1 and plant growth
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: c635000d-4b10-11ee-a964-aac5a93f6ac1
volume: 186
year: '2021'
...
---
_id: '9290'
abstract:
- lang: eng
text: Polar subcellular localization of the PIN exporters of the phytohormone auxin
is a key determinant of directional, intercellular auxin transport and thus a
central topic of both plant cell and developmental biology. Arabidopsis mutants
lacking PID, a kinase that phosphorylates PINs, or the MAB4/MEL proteins of unknown
molecular function display PIN polarity defects and phenocopy pin mutants, but
mechanistic insights into how these factors convey PIN polarity are missing. Here,
by combining protein biochemistry with quantitative live-cell imaging, we demonstrate
that PINs, MAB4/MELs, and AGC kinases interact in the same complex at the plasma
membrane. MAB4/MELs are recruited to the plasma membrane by the PINs and in concert
with the AGC kinases maintain PIN polarity through limiting lateral diffusion-based
escape of PINs from the polar domain. The PIN-MAB4/MEL-PID protein complex has
self-reinforcing properties thanks to positive feedback between AGC kinase-mediated
PIN phosphorylation and MAB4/MEL recruitment. We thus uncover the molecular mechanism
by which AGC kinases and MAB4/MEL proteins regulate PIN localization and plant
development.
acknowledged_ssus:
- _id: Bio
acknowledgement: We acknowledge Ben Scheres, Christian Luschnig, and Claus Schwechheimer
for sharing published material. We thank Monika Hrtyan and Dorota Jaworska at IST
Austria and Gerda Lamers and Ward de Winter at IBL Netherlands for technical assistance;
Corinna Hartinger, Jakub Hajný, Lesia Rodriguez, Mingyue Li, and Lindy Abas for
experimental support; and the Bioimaging Facility at IST Austria and the Bioimaging
Core at VIB for imaging support. We are grateful to Christian Luschnig, Lindy Abas,
and Roman Pleskot for valuable discussions. We also acknowledge the EMBO for supporting
M.G. with a long-term fellowship ( ALTF 1005-2019 ) during the finalization and
revision of this manuscript in the laboratory of B.D.R., and we thank R. Pierik
for allowing K.V.G. to work on this manuscript during a postdoc in his laboratory
at Utrecht University. This work was supported by grants from the European Research
Council under the European Union’s Seventh Framework Programme (ERC grant agreements
742985 to J.F., 714055 to B.D.R., and 803048 to M.F.), the Austrian Science Fund
(FWF; I 3630-B25 to J.F.), Chemical Sciences (partly) financed by the Dutch Research
Council (NWO-CW TOP 700.58.301 to R.O.), the Dutch Research Council (NWO-VICI 865.17.002
to R. Pierik), Grants-in-Aid from the Ministry of Education, Culture, Sports, Science
and Technology, Japan (KAKENHI grant 17K17595 to S.N.), the Ministry of Education,
Youth and Sports of the Czech Republic (MŠMT project NPUI-LO1417 ), and a China
Scholarship Council (to X.W.).
article_processing_charge: No
article_type: original
author:
- first_name: Matous
full_name: Glanc, Matous
id: 1AE1EA24-02D0-11E9-9BAA-DAF4881429F2
last_name: Glanc
orcid: 0000-0003-0619-7783
- first_name: K
full_name: Van Gelderen, K
last_name: Van Gelderen
- first_name: Lukas
full_name: Hörmayer, Lukas
id: 2EEE7A2A-F248-11E8-B48F-1D18A9856A87
last_name: Hörmayer
orcid: 0000-0001-8295-2926
- first_name: Shutang
full_name: Tan, Shutang
id: 2DE75584-F248-11E8-B48F-1D18A9856A87
last_name: Tan
orcid: 0000-0002-0471-8285
- first_name: S
full_name: Naramoto, S
last_name: Naramoto
- first_name: Xixi
full_name: Zhang, Xixi
id: 61A66458-47E9-11EA-85BA-8AEAAF14E49A
last_name: Zhang
orcid: 0000-0001-7048-4627
- first_name: David
full_name: Domjan, David
id: C684CD7A-257E-11EA-9B6F-D8588B4F947F
last_name: Domjan
orcid: 0000-0003-2267-106X
- first_name: L
full_name: Vcelarova, L
last_name: Vcelarova
- first_name: Robert
full_name: Hauschild, Robert
id: 4E01D6B4-F248-11E8-B48F-1D18A9856A87
last_name: Hauschild
orcid: 0000-0001-9843-3522
- 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: E
full_name: de Koning, E
last_name: de Koning
- first_name: M
full_name: van Dop, M
last_name: van Dop
- first_name: E
full_name: Rademacher, E
last_name: Rademacher
- first_name: S
full_name: Janson, S
last_name: Janson
- first_name: X
full_name: Wei, X
last_name: Wei
- first_name: Gergely
full_name: Molnar, Gergely
id: 34F1AF46-F248-11E8-B48F-1D18A9856A87
last_name: Molnar
- first_name: Matyas
full_name: Fendrych, Matyas
id: 43905548-F248-11E8-B48F-1D18A9856A87
last_name: Fendrych
orcid: 0000-0002-9767-8699
- first_name: B
full_name: De Rybel, B
last_name: De Rybel
- first_name: R
full_name: Offringa, R
last_name: Offringa
- first_name: Jiří
full_name: Friml, Jiří
id: 4159519E-F248-11E8-B48F-1D18A9856A87
last_name: Friml
orcid: 0000-0002-8302-7596
citation:
ama: Glanc M, Van Gelderen K, Hörmayer L, et al. AGC kinases and MAB4/MEL proteins
maintain PIN polarity by limiting lateral diffusion in plant cells. Current
Biology. 2021;31(9):1918-1930. doi:10.1016/j.cub.2021.02.028
apa: Glanc, M., Van Gelderen, K., Hörmayer, L., Tan, S., Naramoto, S., Zhang, X.,
… Friml, J. (2021). AGC kinases and MAB4/MEL proteins maintain PIN polarity by
limiting lateral diffusion in plant cells. Current Biology. Elsevier. https://doi.org/10.1016/j.cub.2021.02.028
chicago: Glanc, Matous, K Van Gelderen, Lukas Hörmayer, Shutang Tan, S Naramoto,
Xixi Zhang, David Domjan, et al. “AGC Kinases and MAB4/MEL Proteins Maintain PIN
Polarity by Limiting Lateral Diffusion in Plant Cells.” Current Biology.
Elsevier, 2021. https://doi.org/10.1016/j.cub.2021.02.028.
ieee: M. Glanc et al., “AGC kinases and MAB4/MEL proteins maintain PIN polarity
by limiting lateral diffusion in plant cells,” Current Biology, vol. 31,
no. 9. Elsevier, pp. 1918–1930, 2021.
ista: Glanc M, Van Gelderen K, Hörmayer L, Tan S, Naramoto S, Zhang X, Domjan D,
Vcelarova L, Hauschild R, Johnson AJ, de Koning E, van Dop M, Rademacher E, Janson
S, Wei X, Molnar G, Fendrych M, De Rybel B, Offringa R, Friml J. 2021. AGC kinases
and MAB4/MEL proteins maintain PIN polarity by limiting lateral diffusion in plant
cells. Current Biology. 31(9), 1918–1930.
mla: Glanc, Matous, et al. “AGC Kinases and MAB4/MEL Proteins Maintain PIN Polarity
by Limiting Lateral Diffusion in Plant Cells.” Current Biology, vol. 31,
no. 9, Elsevier, 2021, pp. 1918–30, doi:10.1016/j.cub.2021.02.028.
short: M. Glanc, K. Van Gelderen, L. Hörmayer, S. Tan, S. Naramoto, X. Zhang, D.
Domjan, L. Vcelarova, R. Hauschild, A.J. Johnson, E. de Koning, M. van Dop, E.
Rademacher, S. Janson, X. Wei, G. Molnar, M. Fendrych, B. De Rybel, R. Offringa,
J. Friml, Current Biology 31 (2021) 1918–1930.
date_created: 2021-03-26T12:09:33Z
date_published: 2021-03-10T00:00:00Z
date_updated: 2023-09-05T13:03:34Z
day: '10'
ddc:
- '580'
department:
- _id: JiFr
doi: 10.1016/j.cub.2021.02.028
ec_funded: 1
external_id:
isi:
- '000653077800004'
pmid:
- '33705718'
file:
- access_level: open_access
checksum: b1723040ecfd8c81194185472eb62546
content_type: application/pdf
creator: dernst
date_created: 2021-04-01T10:53:42Z
date_updated: 2021-04-01T10:53:42Z
file_id: '9303'
file_name: 2021_CurrentBiology_Glanc.pdf
file_size: 4324371
relation: main_file
success: 1
file_date_updated: 2021-04-01T10:53:42Z
has_accepted_license: '1'
intvolume: ' 31'
isi: 1
issue: '9'
language:
- iso: eng
month: '03'
oa: 1
oa_version: Published Version
page: 1918-1930
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: 26538374-B435-11E9-9278-68D0E5697425
call_identifier: FWF
grant_number: I03630
name: Molecular mechanisms of endocytic cargo recognition in plants
publication: Current Biology
publication_identifier:
eissn:
- 1879-0445
issn:
- 0960-9822
publication_status: published
publisher: Elsevier
quality_controlled: '1'
status: public
title: AGC kinases and MAB4/MEL proteins maintain PIN polarity by limiting lateral
diffusion in plant cells
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: c635000d-4b10-11ee-a964-aac5a93f6ac1
volume: 31
year: '2021'
...
---
_id: '8824'
abstract:
- lang: eng
text: Plants are able to orient their growth according to gravity, which ultimately
controls both shoot and root architecture.1 Gravitropism is a dynamic process
whereby gravistimulation induces the asymmetric distribution of the plant hormone
auxin, leading to asymmetric growth, organ bending, and subsequent reset of auxin
distribution back to the original pre-gravistimulation situation.1, 2, 3 Differential
auxin accumulation during the gravitropic response depends on the activity of
polarly localized PIN-FORMED (PIN) auxin-efflux carriers.1, 2, 3, 4 In particular,
the timing of this dynamic response is regulated by PIN2,5,6 but the underlying
molecular mechanisms are poorly understood. Here, we show that MEMBRANE ASSOCIATED
KINASE REGULATOR2 (MAKR2) controls the pace of the root gravitropic response.
We found that MAKR2 is required for the PIN2 asymmetry during gravitropism by
acting as a negative regulator of the cell-surface signaling mediated by the receptor-like
kinase TRANSMEMBRANE KINASE1 (TMK1).2,7, 8, 9, 10 Furthermore, we show that
the MAKR2 inhibitory effect on TMK1 signaling is antagonized by auxin itself,
which triggers rapid MAKR2 membrane dissociation in a TMK1-dependent manner. Our
findings suggest that the timing of the root gravitropic response is orchestrated
by the reversible inhibition of the TMK1 signaling pathway at the cell surface.
acknowledgement: "We thank the SiCE group for discussions and comments; S. Yalovsky,
B. Scheres, and the NASC/ABRC collection for providing transgenic Arabidopsis lines
and plasmids; L. Kalmbach and M. Barberon for the gift of pLOK180_pFR7m34GW; A.
Lacroix, J. Berger, and P. Bolland for plant care; and M. Fendrych for help with
microfluidics in the J.F. lab. We acknowledge\r\nthe contribution of the SFR Biosciences
(UMS3444/CNRS, US8/Inser m, ENS de Lyon, UCBL) facilities: C. Lionet, E. Chatre,
and J. Brocard at LBIPLATIM-MICROSCOPY for assistance with imaging, and V. GuegenChaignon
and A. Page at the Protein Science Facility (PSF) for assistance with protein purification
and mass spectrometry. Y.J. was funded by ERC\r\ngrant 3363360-APPL under FP/2007–2013.
Y.J. and Z.L.N. were funded by an ANR- and NSF-supported ERA-CAPS project (SICOPID:
ANR-17-CAPS0003-01/NSF PGRP IOS-1841917). A.I.C.-D. is funded by an ERC consolidator
grant (ERC-2015-CoG–683163) and BIO2016-78955 grant from the Spanish Ministry of
Economy and Competitiveness. Exchanges between the Y.J. and T.B. laboratories were
funded by Tournesol grant 35656NB. B.K.M. was\r\nfunded by the Omics@vib Marie Curie
COFUND and Research Foundation Flanders for a postdoctoral fellowship."
article_processing_charge: Yes (via OA deal)
article_type: original
author:
- first_name: MM
full_name: Marquès-Bueno, MM
last_name: Marquès-Bueno
- first_name: L
full_name: Armengot, L
last_name: Armengot
- first_name: LC
full_name: Noack, LC
last_name: Noack
- first_name: J
full_name: Bareille, J
last_name: Bareille
- 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: MP
full_name: Platre, MP
last_name: Platre
- first_name: V
full_name: Bayle, V
last_name: Bayle
- first_name: M
full_name: Liu, M
last_name: Liu
- first_name: D
full_name: Opdenacker, D
last_name: Opdenacker
- first_name: S
full_name: Vanneste, S
last_name: Vanneste
- first_name: BK
full_name: Möller, BK
last_name: Möller
- first_name: ZL
full_name: Nimchuk, ZL
last_name: Nimchuk
- first_name: T
full_name: Beeckman, T
last_name: Beeckman
- first_name: AI
full_name: Caño-Delgado, AI
last_name: Caño-Delgado
- first_name: Jiří
full_name: Friml, Jiří
id: 4159519E-F248-11E8-B48F-1D18A9856A87
last_name: Friml
orcid: 0000-0002-8302-7596
- first_name: Y
full_name: Jaillais, Y
last_name: Jaillais
citation:
ama: Marquès-Bueno M, Armengot L, Noack L, et al. Auxin-regulated reversible inhibition
of TMK1 signaling by MAKR2 modulates the dynamics of root gravitropism. Current
Biology. 2021;31(1). doi:10.1016/j.cub.2020.10.011
apa: Marquès-Bueno, M., Armengot, L., Noack, L., Bareille, J., Rodriguez Solovey,
L., Platre, M., … Jaillais, Y. (2021). Auxin-regulated reversible inhibition of
TMK1 signaling by MAKR2 modulates the dynamics of root gravitropism. Current
Biology. Elsevier. https://doi.org/10.1016/j.cub.2020.10.011
chicago: Marquès-Bueno, MM, L Armengot, LC Noack, J Bareille, Lesia Rodriguez Solovey,
MP Platre, V Bayle, et al. “Auxin-Regulated Reversible Inhibition of TMK1 Signaling
by MAKR2 Modulates the Dynamics of Root Gravitropism.” Current Biology.
Elsevier, 2021. https://doi.org/10.1016/j.cub.2020.10.011.
ieee: M. Marquès-Bueno et al., “Auxin-regulated reversible inhibition of
TMK1 signaling by MAKR2 modulates the dynamics of root gravitropism,” Current
Biology, vol. 31, no. 1. Elsevier, 2021.
ista: Marquès-Bueno M, Armengot L, Noack L, Bareille J, Rodriguez Solovey L, Platre
M, Bayle V, Liu M, Opdenacker D, Vanneste S, Möller B, Nimchuk Z, Beeckman T,
Caño-Delgado A, Friml J, Jaillais Y. 2021. Auxin-regulated reversible inhibition
of TMK1 signaling by MAKR2 modulates the dynamics of root gravitropism. Current
Biology. 31(1).
mla: Marquès-Bueno, MM, et al. “Auxin-Regulated Reversible Inhibition of TMK1 Signaling
by MAKR2 Modulates the Dynamics of Root Gravitropism.” Current Biology,
vol. 31, no. 1, Elsevier, 2021, doi:10.1016/j.cub.2020.10.011.
short: M. Marquès-Bueno, L. Armengot, L. Noack, J. Bareille, L. Rodriguez Solovey,
M. Platre, V. Bayle, M. Liu, D. Opdenacker, S. Vanneste, B. Möller, Z. Nimchuk,
T. Beeckman, A. Caño-Delgado, J. Friml, Y. Jaillais, Current Biology 31 (2021).
date_created: 2020-12-01T13:39:46Z
date_published: 2021-01-11T00:00:00Z
date_updated: 2023-09-05T13:03:15Z
day: '11'
ddc:
- '570'
department:
- _id: JiFr
doi: 10.1016/j.cub.2020.10.011
external_id:
isi:
- '000614361000039'
pmid:
- '33157019'
file:
- access_level: open_access
checksum: 30b3393d841fb2b1e2b22fb42b5c8fff
content_type: application/pdf
creator: dernst
date_created: 2021-02-04T11:37:50Z
date_updated: 2021-02-04T11:37:50Z
file_id: '9090'
file_name: 2021_CurrentBiology_MarquesBueno.pdf
file_size: 3458646
relation: main_file
success: 1
file_date_updated: 2021-02-04T11:37:50Z
has_accepted_license: '1'
intvolume: ' 31'
isi: 1
issue: '1'
language:
- iso: eng
month: '01'
oa: 1
oa_version: Published Version
pmid: 1
publication: Current Biology
publication_identifier:
eissn:
- 1879-0445
issn:
- 0960-9822
publication_status: published
publisher: Elsevier
quality_controlled: '1'
status: public
title: Auxin-regulated reversible inhibition of TMK1 signaling by MAKR2 modulates
the dynamics of root gravitropism
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: c635000d-4b10-11ee-a964-aac5a93f6ac1
volume: 31
year: '2021'
...