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.
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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
Original language English
Type of outcome Article in a journal
Field of Study 10608 Biochemistry and molecular biology
Country of publisher Germany
Confidentiality degree is not subject to a state or trade secret
WWW 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
Tags CF CELLIM, rivok
Tags International impact, Reviewed
Changed by Changed by: Mgr. Pavla Foltynová, Ph.D., učo 106624. Changed: 26/2/2023 19:40.
Abstract
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
LM2018129, research and development projectName: Národní infrastruktura pro biologické a medicínské zobrazování Czech-BioImaging
Investor: Ministry of Education, Youth and Sports of the CR
PrintDisplayed: 5/5/2024 13:32