PID/WAG-mediated phosphorylation of the Arabidopsis nnnPIN3 auxin transporter mediates polarity switches during gravitropism
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F18%3A73594510" target="_blank" >RIV/61989592:15310/18:73594510 - isvavai.cz</a>
Výsledek na webu
<a href="https://www.nature.com/articles/s41598-018-28188-1" target="_blank" >https://www.nature.com/articles/s41598-018-28188-1</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1038/s41598-018-28188-1" target="_blank" >10.1038/s41598-018-28188-1</a>
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
PID/WAG-mediated phosphorylation of the Arabidopsis nnnPIN3 auxin transporter mediates polarity switches during gravitropism
Popis výsledku v původním jazyce
Intercellular distribution of the plant hormone auxin largely depends on the polar subcellular distribution of the plasma membrane PIN-FORMED (PIN) auxin transporters. PIN polarity switches in response to different developmental and environmental signals have been shown to redirect auxin fluxes mediating certain developmental responses. PIN phosphorylation at different sites and by different kinases is crucial for PIN function. Here we investigate the role of PIN phosphorylation during gravitropic response. Loss-and gain-of-function mutants in PINOID and related kinases but not in D6PK kinase as well as mutations mimicking constitutive dephosphorylated or phosphorylated status of two clusters of predicted phosphorylation sites partially disrupted PIN3 phosphorylation and caused defects in gravitropic bending in roots and hypocotyls. In particular, they impacted PIN3 polarity rearrangements in response to gravity and during feed-back regulation by auxin itself. Thus PIN phosphorylation, besides regulating transport activity and apical-basal targeting, is also important for the rapid polarity switches in response to environmental and endogenous signals.
Název v anglickém jazyce
PID/WAG-mediated phosphorylation of the Arabidopsis nnnPIN3 auxin transporter mediates polarity switches during gravitropism
Popis výsledku anglicky
Intercellular distribution of the plant hormone auxin largely depends on the polar subcellular distribution of the plasma membrane PIN-FORMED (PIN) auxin transporters. PIN polarity switches in response to different developmental and environmental signals have been shown to redirect auxin fluxes mediating certain developmental responses. PIN phosphorylation at different sites and by different kinases is crucial for PIN function. Here we investigate the role of PIN phosphorylation during gravitropic response. Loss-and gain-of-function mutants in PINOID and related kinases but not in D6PK kinase as well as mutations mimicking constitutive dephosphorylated or phosphorylated status of two clusters of predicted phosphorylation sites partially disrupted PIN3 phosphorylation and caused defects in gravitropic bending in roots and hypocotyls. In particular, they impacted PIN3 polarity rearrangements in response to gravity and during feed-back regulation by auxin itself. Thus PIN phosphorylation, besides regulating transport activity and apical-basal targeting, is also important for the rapid polarity switches in response to environmental and endogenous signals.
Klasifikace
Druh
J<sub>imp</sub> - Článek v periodiku v databázi Web of Science
CEP obor
—
OECD FORD obor
10608 - Biochemistry and molecular biology
Návaznosti výsledku
Projekt
—
Návaznosti
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Ostatní
Rok uplatnění
2018
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
Scientific Reports
ISSN
2045-2322
e-ISSN
—
Svazek periodika
8
Číslo periodika v rámci svazku
JUL
Stát vydavatele periodika
GB - Spojené království Velké Británie a Severního Irska
Počet stran výsledku
11
Strana od-do
"10279-1"-"10279-11"
Kód UT WoS článku
000437673200053
EID výsledku v databázi Scopus
2-s2.0-85049617694