---
_id: '8992'
abstract:
- lang: eng
text: The phytohormone auxin plays a central role in shaping plant growth and development.
With decades of genetic and biochemical studies, numerous core molecular components
and their networks, underlying auxin biosynthesis, transport, and signaling, have
been identified. Notably, protein phosphorylation, catalyzed by kinases and oppositely
hydrolyzed by phosphatases, has been emerging to be a crucial type of post-translational
modification, regulating physiological and developmental auxin output at all levels.
In this review, we comprehensively discuss earlier and recent advances in our
understanding of genetics, biochemistry, and cell biology of the kinases and phosphatases
participating in auxin action. We provide insights into the mechanisms by which
reversible protein phosphorylation defines developmental auxin responses, discuss
current challenges, and provide our perspectives on future directions involving
the integration of the control of protein phosphorylation into the molecular auxin
network.
acknowledgement: This work was supported by the European Union’s Horizon 2020 Program
(ERC grant agreement no. 742985 to J.F.). S.T. was funded by a European Molecular
Biology Organization (EMBO) long-term postdoctoral fellowship (ALTF 723-2015). C.L.
is supported by the Austrian Science Fund (FWF; P 31493).
article_processing_charge: No
article_type: original
author:
- first_name: Shutang
full_name: Tan, Shutang
id: 2DE75584-F248-11E8-B48F-1D18A9856A87
last_name: Tan
orcid: 0000-0002-0471-8285
- first_name: Christian
full_name: Luschnig, Christian
last_name: Luschnig
- first_name: Jiří
full_name: Friml, Jiří
id: 4159519E-F248-11E8-B48F-1D18A9856A87
last_name: Friml
orcid: 0000-0002-8302-7596
citation:
ama: 'Tan S, Luschnig C, Friml J. Pho-view of auxin: Reversible protein phosphorylation
in auxin biosynthesis, transport and signaling. Molecular Plant. 2021;14(1):151-165.
doi:10.1016/j.molp.2020.11.004'
apa: 'Tan, S., Luschnig, C., & Friml, J. (2021). Pho-view of auxin: Reversible
protein phosphorylation in auxin biosynthesis, transport and signaling. Molecular
Plant. Elsevier. https://doi.org/10.1016/j.molp.2020.11.004'
chicago: 'Tan, Shutang, Christian Luschnig, and Jiří Friml. “Pho-View of Auxin:
Reversible Protein Phosphorylation in Auxin Biosynthesis, Transport and Signaling.”
Molecular Plant. Elsevier, 2021. https://doi.org/10.1016/j.molp.2020.11.004.'
ieee: 'S. Tan, C. Luschnig, and J. Friml, “Pho-view of auxin: Reversible protein
phosphorylation in auxin biosynthesis, transport and signaling,” Molecular
Plant, vol. 14, no. 1. Elsevier, pp. 151–165, 2021.'
ista: 'Tan S, Luschnig C, Friml J. 2021. Pho-view of auxin: Reversible protein phosphorylation
in auxin biosynthesis, transport and signaling. Molecular Plant. 14(1), 151–165.'
mla: 'Tan, Shutang, et al. “Pho-View of Auxin: Reversible Protein Phosphorylation
in Auxin Biosynthesis, Transport and Signaling.” Molecular Plant, vol.
14, no. 1, Elsevier, 2021, pp. 151–65, doi:10.1016/j.molp.2020.11.004.'
short: S. Tan, C. Luschnig, J. Friml, Molecular Plant 14 (2021) 151–165.
date_created: 2021-01-03T23:01:23Z
date_published: 2021-01-04T00:00:00Z
date_updated: 2023-08-04T11:21:13Z
day: '04'
ddc:
- '580'
department:
- _id: JiFr
doi: 10.1016/j.molp.2020.11.004
ec_funded: 1
external_id:
isi:
- '000605359400014'
pmid:
- '33186755'
file:
- access_level: open_access
checksum: 917e60e57092f22e16beac70b1775ea6
content_type: application/pdf
creator: dernst
date_created: 2021-01-07T14:03:53Z
date_updated: 2021-01-07T14:03:53Z
file_id: '8995'
file_name: 2020_MolecularPlant_Tan.pdf
file_size: 871088
relation: main_file
success: 1
file_date_updated: 2021-01-07T14:03:53Z
has_accepted_license: '1'
intvolume: ' 14'
isi: 1
issue: '1'
language:
- iso: eng
month: '01'
oa: 1
oa_version: Published Version
page: 151-165
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: 256FEF10-B435-11E9-9278-68D0E5697425
grant_number: 723-2015
name: Long Term Fellowship
publication: Molecular Plant
publication_identifier:
eissn:
- '17529867'
issn:
- '16742052'
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: 'Pho-view of auxin: Reversible protein phosphorylation in auxin biosynthesis,
transport and signaling'
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: 14
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
license: https://creativecommons.org/licenses/by-nc-nd/4.0/
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: '8943'
abstract:
- lang: eng
text: The widely used non-steroidal anti-inflammatory drugs (NSAIDs) are derivatives
of the phytohormone salicylic acid (SA). SA is well known to regulate plant immunity
and development, whereas there have been few reports focusing on the effects of
NSAIDs in plants. Our studies here reveal that NSAIDs exhibit largely overlapping
physiological activities to SA in the model plant Arabidopsis. NSAID treatments
lead to shorter and agravitropic primary roots and inhibited lateral root organogenesis.
Notably, in addition to the SA-like action, which in roots involves binding to
the protein phosphatase 2A (PP2A), NSAIDs also exhibit PP2A-independent effects.
Cell biological and biochemical analyses reveal that many NSAIDs bind directly
to and inhibit the chaperone activity of TWISTED DWARF1, thereby regulating actin
cytoskeleton dynamics and subsequent endosomal trafficking. Our findings uncover
an unexpected bioactivity of human pharmaceuticals in plants and provide insights
into the molecular mechanism underlying the cellular action of this class of anti-inflammatory
compounds.
acknowledged_ssus:
- _id: LifeSc
- _id: Bio
acknowledgement: "We thank Drs. Sebastian Bednarek (University of Wisconsin-Madison),
Niko Geldner (University of Lausanne), and Karin Schumacher (Heidelberg University)
for kindly sharing published Arabidopsis lines; Dr. Satoshi Naramoto for the pPIN2::PIN2-GFP;
pVHA-a1::VHA-a1-mRFP reporter; the staff at the Life Science Facility and Bioimaging
Facility, Monika Hrtyan, and Dorota Jaworska at IST Austria for technical support;
and Drs. Su Tang (Texas A&M University),\r\nMelinda Abas (BOKU), Eva Benkova´ (IST
Austria), Christian Luschnig (BOKU), Bartel Vanholme (Gent University), and the
Friml group for valuable discussions. The research leading to these findings was
funded by the European Union’s Horizon 2020 program (ERC grant agreement no. 742985,
to J.F.), the People Programme (Marie Curie Actions) of the European Union’s Seventh
Framework Programme (FP7/2007-2013) under REA grant agreement no.\r\n291734, the
Swiss National Funds (31003A_165877, to M.G.), the Ministry of Education, Youth,
and Sports of the Czech Republic (project no. CZ.02.1.01/0.0/0.0/16_019/0000738,
EU Operational Programme ‘‘Research, development and education and Centre for Plant
Experimental Biology’’), and the EU Operational Programme Prague - Competitiveness
(project no. CZ.2.16/3.1.00/21519). S.T. was funded by a European Molecular Biology
Organization (EMBO) long-term postdoctoral fellowship (ALTF 723-2015). X.Z. was
partly supported by a PhD scholarship from the China Scholarship Council."
article_number: '108463'
article_processing_charge: Yes
article_type: original
author:
- first_name: Shutang
full_name: Tan, Shutang
id: 2DE75584-F248-11E8-B48F-1D18A9856A87
last_name: Tan
orcid: 0000-0002-0471-8285
- first_name: Martin
full_name: Di Donato, Martin
last_name: Di Donato
- first_name: Matous
full_name: Glanc, Matous
id: 1AE1EA24-02D0-11E9-9BAA-DAF4881429F2
last_name: Glanc
orcid: 0000-0003-0619-7783
- first_name: Xixi
full_name: Zhang, Xixi
id: 61A66458-47E9-11EA-85BA-8AEAAF14E49A
last_name: Zhang
orcid: 0000-0001-7048-4627
- first_name: Petr
full_name: Klíma, Petr
last_name: Klíma
- first_name: Jie
full_name: Liu, Jie
last_name: Liu
- first_name: Aurélien
full_name: Bailly, Aurélien
last_name: Bailly
- first_name: Noel
full_name: Ferro, Noel
last_name: Ferro
- first_name: Jan
full_name: Petrášek, Jan
last_name: Petrášek
- first_name: Markus
full_name: Geisler, Markus
last_name: Geisler
- first_name: Jiří
full_name: Friml, Jiří
id: 4159519E-F248-11E8-B48F-1D18A9856A87
last_name: Friml
orcid: 0000-0002-8302-7596
citation:
ama: Tan S, Di Donato M, Glanc M, et al. Non-steroidal anti-inflammatory drugs target
TWISTED DWARF1-regulated actin dynamics and auxin transport-mediated plant development.
Cell Reports. 2020;33(9). doi:10.1016/j.celrep.2020.108463
apa: Tan, S., Di Donato, M., Glanc, M., Zhang, X., Klíma, P., Liu, J., … Friml,
J. (2020). Non-steroidal anti-inflammatory drugs target TWISTED DWARF1-regulated
actin dynamics and auxin transport-mediated plant development. Cell Reports.
Elsevier. https://doi.org/10.1016/j.celrep.2020.108463
chicago: Tan, Shutang, Martin Di Donato, Matous Glanc, Xixi Zhang, Petr Klíma, Jie
Liu, Aurélien Bailly, et al. “Non-Steroidal Anti-Inflammatory Drugs Target TWISTED
DWARF1-Regulated Actin Dynamics and Auxin Transport-Mediated Plant Development.”
Cell Reports. Elsevier, 2020. https://doi.org/10.1016/j.celrep.2020.108463.
ieee: S. Tan et al., “Non-steroidal anti-inflammatory drugs target TWISTED
DWARF1-regulated actin dynamics and auxin transport-mediated plant development,”
Cell Reports, vol. 33, no. 9. Elsevier, 2020.
ista: Tan S, Di Donato M, Glanc M, Zhang X, Klíma P, Liu J, Bailly A, Ferro N, Petrášek
J, Geisler M, Friml J. 2020. Non-steroidal anti-inflammatory drugs target TWISTED
DWARF1-regulated actin dynamics and auxin transport-mediated plant development.
Cell Reports. 33(9), 108463.
mla: Tan, Shutang, et al. “Non-Steroidal Anti-Inflammatory Drugs Target TWISTED
DWARF1-Regulated Actin Dynamics and Auxin Transport-Mediated Plant Development.”
Cell Reports, vol. 33, no. 9, 108463, Elsevier, 2020, doi:10.1016/j.celrep.2020.108463.
short: S. Tan, M. Di Donato, M. Glanc, X. Zhang, P. Klíma, J. Liu, A. Bailly, N.
Ferro, J. Petrášek, M. Geisler, J. Friml, Cell Reports 33 (2020).
date_created: 2020-12-13T23:01:21Z
date_published: 2020-12-01T00:00:00Z
date_updated: 2023-11-16T13:03:31Z
day: '01'
ddc:
- '580'
department:
- _id: JiFr
doi: 10.1016/j.celrep.2020.108463
ec_funded: 1
external_id:
isi:
- '000595658100018'
pmid:
- '33264621'
file:
- access_level: open_access
checksum: ed18cba0fb48ed2e789381a54cc21904
content_type: application/pdf
creator: dernst
date_created: 2020-12-14T07:33:39Z
date_updated: 2020-12-14T07:33:39Z
file_id: '8948'
file_name: 2020_CellReports_Tan.pdf
file_size: 8056434
relation: main_file
success: 1
file_date_updated: 2020-12-14T07:33:39Z
has_accepted_license: '1'
intvolume: ' 33'
isi: 1
issue: '9'
language:
- iso: eng
month: '12'
oa: 1
oa_version: Published Version
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: 25681D80-B435-11E9-9278-68D0E5697425
call_identifier: FP7
grant_number: '291734'
name: International IST Postdoc Fellowship Programme
- _id: 256FEF10-B435-11E9-9278-68D0E5697425
grant_number: 723-2015
name: Long Term Fellowship
publication: Cell Reports
publication_identifier:
eissn:
- '22111247'
publication_status: published
publisher: Elsevier
quality_controlled: '1'
related_material:
link:
- description: News on IST Homepage
relation: press_release
url: https://ist.ac.at/en/news/plants-on-aspirin/
scopus_import: '1'
status: public
title: Non-steroidal anti-inflammatory drugs target TWISTED DWARF1-regulated actin
dynamics and auxin transport-mediated plant development
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: 33
year: '2020'
...
---
_id: '7427'
abstract:
- lang: eng
text: Plants, like other multicellular organisms, survive through a delicate balance
between growth and defense against pathogens. Salicylic acid (SA) is a major defense
signal in plants, and the perception mechanism as well as downstream signaling
activating the immune response are known. Here, we identify a parallel SA signaling
that mediates growth attenuation. SA directly binds to A subunits of protein phosphatase
2A (PP2A), inhibiting activity of this complex. Among PP2A targets, the PIN2 auxin
transporter is hyperphosphorylated in response to SA, leading to changed activity
of this important growth regulator. Accordingly, auxin transport and auxin-mediated
root development, including growth, gravitropic response, and lateral root organogenesis,
are inhibited. This study reveals how SA, besides activating immunity, concomitantly
attenuates growth through crosstalk with the auxin distribution network. Further
analysis of this dual role of SA and characterization of additional SA-regulated
PP2A targets will provide further insights into mechanisms maintaining a balance
between growth and defense.
acknowledged_ssus:
- _id: Bio
- _id: LifeSc
acknowledgement: "We thank Shigeyuki Betsuyaku (University of Tsukuba), Alison Delong
(Brown University), Xinnian Dong (Duke University), Dolf Weijers (Wageningen University),
Yuelin Zhang (UBC), and Martine Pastuglia (Institut Jean-Pierre Bourgin) for sharing
published materials; Jana Riederer for help with cantharidin physiological analysis;
David Domjan for help with cloning pET28a-PIN2HL; Qing Lu for help with DARTS; Hana
Kozubı´kova´ for technical support on SA derivative synthesis; Zuzana Vondra´ kova´
for technical support with tobacco cells; Lucia Strader (Washington University),
Bert De Rybel (Ghent University), Bartel Vanholme (Ghent University), and Lukas
Mach (BOKU) for helpful discussions; and bioimaging and life science facilities
of IST Austria for continuous support. We gratefully acknowledge the Nottingham
Arabidopsis Stock Center (NASC) for providing T-DNA insertional mutants. The DSC
and SPR instruments were provided by the EQ-BOKU VIBT GmbH and the BOKU Core Facility
for Biomolecular and Cellular Analysis, with help of Irene Schaffner. The research
leading to these results has received funding from the European Union’s Horizon
2020 program (ERC grant agreement no. 742985 to J.F.) and the People Programme (Marie
Curie Actions) of the European Union’s Seventh Framework Programme (FP7/2007-2013)
under REA grant agreement no. 291734. S.T. was supported by a European Molecular
Biology Organization (EMBO) long-term postdoctoral fellowship (ALTF 723-2015). O.N.
was supported by the Ministry of Education, Youth and Sports of the Czech Republic
(European Regional Development Fund-Project ‘‘Centre for Experimental Plant Biology’’
no. CZ.02.1.01/0.0/0.0/16_019/0000738). J. Pospısil was supported by European Regional
Development Fund Project ‘‘Centre for Experimental Plant Biology’’\r\n(no. CZ.02.1.01/0.0/0.0/16_019/0000738).
J. Petrasek was supported by EU Operational Programme Prague-Competitiveness (no.
CZ.2.16/3.1.00/21519). "
article_processing_charge: No
article_type: original
author:
- first_name: Shutang
full_name: Tan, Shutang
id: 2DE75584-F248-11E8-B48F-1D18A9856A87
last_name: Tan
orcid: 0000-0002-0471-8285
- first_name: Melinda F
full_name: Abas, Melinda F
id: 3CFB3B1C-F248-11E8-B48F-1D18A9856A87
last_name: Abas
- first_name: Inge
full_name: Verstraeten, Inge
id: 362BF7FE-F248-11E8-B48F-1D18A9856A87
last_name: Verstraeten
orcid: 0000-0001-7241-2328
- first_name: Matous
full_name: Glanc, Matous
id: 1AE1EA24-02D0-11E9-9BAA-DAF4881429F2
last_name: Glanc
orcid: 0000-0003-0619-7783
- first_name: Gergely
full_name: Molnar, Gergely
id: 34F1AF46-F248-11E8-B48F-1D18A9856A87
last_name: Molnar
- first_name: Jakub
full_name: Hajny, Jakub
id: 4800CC20-F248-11E8-B48F-1D18A9856A87
last_name: Hajny
orcid: 0000-0003-2140-7195
- first_name: Pavel
full_name: Lasák, Pavel
last_name: Lasák
- first_name: Ivan
full_name: Petřík, Ivan
last_name: Petřík
- first_name: Eugenia
full_name: Russinova, Eugenia
last_name: Russinova
- first_name: Jan
full_name: Petrášek, Jan
last_name: Petrášek
- first_name: Ondřej
full_name: Novák, Ondřej
last_name: Novák
- first_name: Jiří
full_name: Pospíšil, Jiří
last_name: Pospíšil
- first_name: Jiří
full_name: Friml, Jiří
id: 4159519E-F248-11E8-B48F-1D18A9856A87
last_name: Friml
orcid: 0000-0002-8302-7596
citation:
ama: Tan S, Abas MF, Verstraeten I, et al. Salicylic acid targets protein phosphatase
2A to attenuate growth in plants. Current Biology. 2020;30(3):381-395.e8.
doi:10.1016/j.cub.2019.11.058
apa: Tan, S., Abas, M. F., Verstraeten, I., Glanc, M., Molnar, G., Hajny, J., …
Friml, J. (2020). Salicylic acid targets protein phosphatase 2A to attenuate growth
in plants. Current Biology. Cell Press. https://doi.org/10.1016/j.cub.2019.11.058
chicago: Tan, Shutang, Melinda F Abas, Inge Verstraeten, Matous Glanc, Gergely Molnar,
Jakub Hajny, Pavel Lasák, et al. “Salicylic Acid Targets Protein Phosphatase 2A
to Attenuate Growth in Plants.” Current Biology. Cell Press, 2020. https://doi.org/10.1016/j.cub.2019.11.058.
ieee: S. Tan et al., “Salicylic acid targets protein phosphatase 2A to attenuate
growth in plants,” Current Biology, vol. 30, no. 3. Cell Press, p. 381–395.e8,
2020.
ista: Tan S, Abas MF, Verstraeten I, Glanc M, Molnar G, Hajny J, Lasák P, Petřík
I, Russinova E, Petrášek J, Novák O, Pospíšil J, Friml J. 2020. Salicylic acid
targets protein phosphatase 2A to attenuate growth in plants. Current Biology.
30(3), 381–395.e8.
mla: Tan, Shutang, et al. “Salicylic Acid Targets Protein Phosphatase 2A to Attenuate
Growth in Plants.” Current Biology, vol. 30, no. 3, Cell Press, 2020, p.
381–395.e8, doi:10.1016/j.cub.2019.11.058.
short: S. Tan, M.F. Abas, I. Verstraeten, M. Glanc, G. Molnar, J. Hajny, P. Lasák,
I. Petřík, E. Russinova, J. Petrášek, O. Novák, J. Pospíšil, J. Friml, Current
Biology 30 (2020) 381–395.e8.
date_created: 2020-02-02T23:01:00Z
date_published: 2020-02-03T00:00:00Z
date_updated: 2024-03-25T23:30:20Z
day: '03'
ddc:
- '580'
department:
- _id: JiFr
- _id: EvBe
doi: 10.1016/j.cub.2019.11.058
ec_funded: 1
external_id:
isi:
- '000511287900018'
pmid:
- '31956021'
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creator: dernst
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language:
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month: '02'
oa: 1
oa_version: Published Version
page: 381-395.e8
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: 25681D80-B435-11E9-9278-68D0E5697425
call_identifier: FP7
grant_number: '291734'
name: International IST Postdoc Fellowship Programme
- _id: 256FEF10-B435-11E9-9278-68D0E5697425
grant_number: 723-2015
name: Long Term Fellowship
publication: Current Biology
publication_identifier:
issn:
- '09609822'
publication_status: published
publisher: Cell Press
quality_controlled: '1'
related_material:
record:
- id: '8822'
relation: dissertation_contains
status: public
scopus_import: '1'
status: public
title: Salicylic acid targets protein phosphatase 2A to attenuate growth in plants
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: 30
year: '2020'
...
---
_id: '7600'
abstract:
- lang: eng
text: Directional intercellular transport of the phytohormone auxin mediated by
PIN FORMED (PIN) efflux carriers plays essential roles in both coordinating patterning
processes and integrating multiple external cues by rapidly redirecting auxin
fluxes. Multilevel regulations of PIN activity under internal and external cues
are complicated; however, the underlying molecular mechanism remains elusive.
Here we demonstrate that 3’-Phosphoinositide-Dependent Protein Kinase1 (PDK1),
which is conserved in plants and mammals, functions as a molecular hub integrating
the upstream lipid signalling and the downstream substrate activity through phosphorylation.
Genetic analysis uncovers that loss-of-function Arabidopsis mutant pdk1.1 pdk1.2
exhibits a plethora of abnormalities in organogenesis and growth, due to the defective
PIN-dependent auxin transport. Further cellular and biochemical analyses reveal
that PDK1 phosphorylates D6 Protein Kinase to facilitate its activity towards
PIN proteins. Our studies establish a lipid-dependent phosphorylation cascade
connecting membrane composition-based cellular signalling with plant growth and
patterning by regulating morphogenetic auxin fluxes.
acknowledged_ssus:
- _id: Bio
- _id: LifeSc
article_processing_charge: No
article_type: original
author:
- first_name: Shutang
full_name: Tan, Shutang
id: 2DE75584-F248-11E8-B48F-1D18A9856A87
last_name: Tan
orcid: 0000-0002-0471-8285
- first_name: Xixi
full_name: Zhang, Xixi
id: 61A66458-47E9-11EA-85BA-8AEAAF14E49A
last_name: Zhang
orcid: 0000-0001-7048-4627
- first_name: Wei
full_name: Kong, Wei
last_name: Kong
- first_name: Xiao-Li
full_name: Yang, Xiao-Li
last_name: Yang
- first_name: Gergely
full_name: Molnar, Gergely
id: 34F1AF46-F248-11E8-B48F-1D18A9856A87
last_name: Molnar
- first_name: Zuzana
full_name: Vondráková, Zuzana
last_name: Vondráková
- first_name: Roberta
full_name: Filepová, Roberta
last_name: Filepová
- first_name: Jan
full_name: Petrášek, Jan
last_name: Petrášek
- first_name: Jiří
full_name: Friml, Jiří
id: 4159519E-F248-11E8-B48F-1D18A9856A87
last_name: Friml
orcid: 0000-0002-8302-7596
- first_name: Hong-Wei
full_name: Xue, Hong-Wei
last_name: Xue
citation:
ama: Tan S, Zhang X, Kong W, et al. The lipid code-dependent phosphoswitch PDK1–D6PK
activates PIN-mediated auxin efflux in Arabidopsis. Nature Plants. 2020;6:556-569.
doi:10.1038/s41477-020-0648-9
apa: Tan, S., Zhang, X., Kong, W., Yang, X.-L., Molnar, G., Vondráková, Z., … Xue,
H.-W. (2020). The lipid code-dependent phosphoswitch PDK1–D6PK activates PIN-mediated
auxin efflux in Arabidopsis. Nature Plants. Springer Nature. https://doi.org/10.1038/s41477-020-0648-9
chicago: Tan, Shutang, Xixi Zhang, Wei Kong, Xiao-Li Yang, Gergely Molnar, Zuzana
Vondráková, Roberta Filepová, Jan Petrášek, Jiří Friml, and Hong-Wei Xue. “The
Lipid Code-Dependent Phosphoswitch PDK1–D6PK Activates PIN-Mediated Auxin Efflux
in Arabidopsis.” Nature Plants. Springer Nature, 2020. https://doi.org/10.1038/s41477-020-0648-9.
ieee: S. Tan et al., “The lipid code-dependent phosphoswitch PDK1–D6PK activates
PIN-mediated auxin efflux in Arabidopsis,” Nature Plants, vol. 6. Springer
Nature, pp. 556–569, 2020.
ista: Tan S, Zhang X, Kong W, Yang X-L, Molnar G, Vondráková Z, Filepová R, Petrášek
J, Friml J, Xue H-W. 2020. The lipid code-dependent phosphoswitch PDK1–D6PK activates
PIN-mediated auxin efflux in Arabidopsis. Nature Plants. 6, 556–569.
mla: Tan, Shutang, et al. “The Lipid Code-Dependent Phosphoswitch PDK1–D6PK Activates
PIN-Mediated Auxin Efflux in Arabidopsis.” Nature Plants, vol. 6, Springer
Nature, 2020, pp. 556–69, doi:10.1038/s41477-020-0648-9.
short: S. Tan, X. Zhang, W. Kong, X.-L. Yang, G. Molnar, Z. Vondráková, R. Filepová,
J. Petrášek, J. Friml, H.-W. Xue, Nature Plants 6 (2020) 556–569.
date_created: 2020-03-21T16:34:16Z
date_published: 2020-05-01T00:00:00Z
date_updated: 2023-08-18T07:05:57Z
day: '01'
department:
- _id: JiFr
doi: 10.1038/s41477-020-0648-9
ec_funded: 1
external_id:
isi:
- '000531787500006'
pmid:
- '32393881'
intvolume: ' 6'
isi: 1
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1101/755504
month: '05'
oa: 1
oa_version: Preprint
page: 556-569
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: 256FEF10-B435-11E9-9278-68D0E5697425
grant_number: 723-2015
name: Long Term Fellowship
publication: Nature Plants
publication_identifier:
eissn:
- '20550278'
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
related_material:
link:
- relation: erratum
url: https://doi.org/10.1038/s41477-020-0719-y
scopus_import: '1'
status: public
title: The lipid code-dependent phosphoswitch PDK1–D6PK activates PIN-mediated auxin
efflux in Arabidopsis
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 6
year: '2020'
...