ABP1-TMK auxin perception for global phosphorylation and auxin canalization

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F22%3A00128524" target="_blank" >RIV/00216224:14740/22:00128524 - isvavai.cz</a>

Výsledek na webu

<a href="https://www.nature.com/articles/s41586-022-05187-x" target="_blank" >https://www.nature.com/articles/s41586-022-05187-x</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1038/s41586-022-05187-x" target="_blank" >10.1038/s41586-022-05187-x</a>

Jazyk výsledku

angličtina

Název v původním jazyce

ABP1-TMK auxin perception for global phosphorylation and auxin canalization

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

ABP1-TMK auxin perception for global phosphorylation and auxin canalization

Popis výsledku anglicky

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.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10608 - Biochemistry and molecular biology

Projekt

<a href="/cs/project/LM2018129" target="_blank" >LM2018129: Národní infrastruktura pro biologické a medicínské zobrazování Czech-BioImaging</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2022

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Nature

ISSN

0028-0836

e-ISSN

—

Svazek periodika

609

Číslo periodika v rámci svazku

7927

Stát vydavatele periodika

DE - Spolková republika Německo

Počet stran výsledku

26

Strana od-do

575-581

Kód UT WoS článku

000851357500002

EID výsledku v databázi Scopus

2-s2.0-85137529859