ABP1-TMK auxin perception for global phosphorylation and auxin
canalization

J 2022

ABP1-TMK auxin perception for global phosphorylation and auxin canalization

FRIML, Jiri, Michelle GALLEI, Zuzana GELOVA, Alexander JOHNSON, Ewa MAZUR et. al.

Basic information

Original name

ABP1-TMK auxin perception for global phosphorylation and auxin canalization

Authors

FRIML, Jiri, Michelle GALLEI, Zuzana GELOVA, Alexander JOHNSON, Ewa MAZUR, Aline MONZER, Lesia RODRIGUEZ, Mark ROOSJEN, Inge VERSTRAETEN, Branka D ZIVANOVIC, Minxia ZOU, Lukas FIEDLER, Caterina GIANNINI, Peter GRONES, Monika HRTYAN, Walter A KAUFMANN, Andre KUHN, Madhumitha NARASIMHAN, Marek RANDUCH, Nikola RÝDZA (703 Slovakia, guarantor, belonging to the institution), Koji TAKAHASHI, Shutang TAN, Anastasia TEPLOVA, Toshinori KINOSHITA, Dolf WEIJERS and Hana RAKUSOVA

Edition

Nature, LONDON, NATURE PUBLISHING GROUP, 2022, 0028-0836

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10608 Biochemistry and molecular biology

Country of publisher

Germany

Confidentiality degree

není předmětem státního či obchodního tajemství

References:

URL

Impact factor

Impact factor: 64.800

RIV identification code

RIV/00216224:14740/22:00128524

Organization unit

Central European Institute of Technology

DOI

http://dx.doi.org/10.1038/s41586-022-05187-x

UT WoS

000851357500002

Keywords in English

BINDING PROTEIN-1ARABIDOPSISTRANSPORTGRADIENTSCOMPLEXMODULEGROWTH

Abstract

V originále

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 unclear(1-3). Whether auxin-binding protein 1 (ABP1) is an auxin receptor has been a source of debate for decades(1,4). 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.

Links

90129, large research infrastructures

Name: Czech-BioImaging II

Citovat

FRIML, Jiri, Michelle GALLEI, Zuzana GELOVA, Alexander JOHNSON, Ewa MAZUR, Aline MONZER, Lesia RODRIGUEZ, Mark ROOSJEN, Inge VERSTRAETEN, Branka D ZIVANOVIC, Minxia ZOU, Lukas FIEDLER, Caterina GIANNINI, Peter GRONES, Monika HRTYAN, Walter A KAUFMANN, Andre KUHN, Madhumitha NARASIMHAN, Marek RANDUCH, Nikola RÝDZA, Koji TAKAHASHI, Shutang TAN, Anastasia TEPLOVA, Toshinori KINOSHITA, Dolf WEIJERS and Hana RAKUSOVA. ABP1-TMK auxin perception for global phosphorylation and auxin canalization. Nature. LONDON: NATURE PUBLISHING GROUP, 2022, vol. 609, No 7927, p. 575-581, 26 pp. ISSN 0028-0836. Available from: https://dx.doi.org/10.1038/s41586-022-05187-x.

@article{2252406,
   author = {Friml, Jiri and Gallei, Michelle and Gelova, Zuzana and Johnson, Alexander and Mazur, Ewa and Monzer, Aline and Rodriguez, Lesia and Roosjen, Mark and Verstraeten, Inge and Zivanovic, Branka D and Zou, Minxia and Fiedler, Lukas and Giannini, Caterina and Grones, Peter and Hrtyan, Monika and Kaufmann, Walter A and Kuhn, Andre and Narasimhan, Madhumitha and Randuch, Marek and Rýdza, Nikola and Takahashi, Koji and Tan, Shutang and Teplova, Anastasia and Kinoshita, Toshinori and Weijers, Dolf and Rakusova, Hana},
   article_location = {LONDON},
   article_number = {7927},
   doi = {http://dx.doi.org/10.1038/s41586-022-05187-x},
   keywords = {BINDING PROTEIN-1ARABIDOPSISTRANSPORTGRADIENTSCOMPLEXMODULEGROWTH},
   language = {eng},
   issn = {0028-0836},
   journal = {Nature},
   title = {ABP1-TMK auxin perception for global phosphorylation and auxin canalization},
   url = {https://www.nature.com/articles/s41586-022-05187-x},
   volume = {609},
   year = {2022}
}

TY  - JOUR
ID  - 2252406
AU  - Friml, Jiri - Gallei, Michelle - Gelova, Zuzana - Johnson, Alexander - Mazur, Ewa - Monzer, Aline - Rodriguez, Lesia - Roosjen, Mark - Verstraeten, Inge - Zivanovic, Branka D - Zou, Minxia - Fiedler, Lukas - Giannini, Caterina - Grones, Peter - Hrtyan, Monika - Kaufmann, Walter A - Kuhn, Andre - Narasimhan, Madhumitha - Randuch, Marek - Rýdza, Nikola - Takahashi, Koji - Tan, Shutang - Teplova, Anastasia - Kinoshita, Toshinori - Weijers, Dolf - Rakusova, Hana
PY  - 2022
TI  - ABP1-TMK auxin perception for global phosphorylation and auxin canalization
JF  - Nature
VL  - 609
IS  - 7927
SP  - 575-581
EP  - 575-581
PB  - NATURE PUBLISHING GROUP
SN  - 00280836
KW  - BINDING PROTEIN-1ARABIDOPSISTRANSPORTGRADIENTSCOMPLEXMODULEGROWTH
UR  - https://www.nature.com/articles/s41586-022-05187-x
N2  - 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 unclear(1-3). Whether auxin-binding protein 1 (ABP1) is an auxin receptor has been a source of debate for decades(1,4). 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.
ER  -

FRIML, Jiri, Michelle GALLEI, Zuzana GELOVA, Alexander JOHNSON, Ewa MAZUR, Aline MONZER, Lesia RODRIGUEZ, Mark ROOSJEN, Inge VERSTRAETEN, Branka D ZIVANOVIC, Minxia ZOU, Lukas FIEDLER, Caterina GIANNINI, Peter GRONES, Monika HRTYAN, Walter A KAUFMANN, Andre KUHN, Madhumitha NARASIMHAN, Marek RANDUCH, Nikola RÝDZA, Koji TAKAHASHI, Shutang TAN, Anastasia TEPLOVA, Toshinori KINOSHITA, Dolf WEIJERS and Hana RAKUSOVA. ABP1-TMK auxin perception for global phosphorylation and auxin canalization. \textit{Nature}. LONDON: NATURE PUBLISHING GROUP, 2022, vol.~609, No~7927, p.~575-581, 26 pp. ISSN~0028-0836. Available from: https://dx.doi.org/10.1038/s41586-022-05187-x.

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