The dynamics and endocytosis of Flot1 protein in response to flg22 in Arabidopsis

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F17%3A73583635" target="_blank" >RIV/61989592:15310/17:73583635 - isvavai.cz</a>

Výsledek na webu

<a href="http://www.sciencedirect.com/science/article/pii/S017616171730130X" target="_blank" >http://www.sciencedirect.com/science/article/pii/S017616171730130X</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.jplph.2017.05.010" target="_blank" >10.1016/j.jplph.2017.05.010</a>

Jazyk výsledku

angličtina

Název v původním jazyce

The dynamics and endocytosis of Flot1 protein in response to flg22 in Arabidopsis

Popis výsledku v původním jazyce

Membrane microdomains play vital roles in the process of bacterial infection. The membrane microdomain associated protein Flot1 acts in an endocytic pathway and is required for seedling development, however, whether Flot1 is a part of host defense mechanisms remains unknown. During an analysis of callose deposition, we found that Flot1 amiRNAi mutants exhibited defects in response to flg22. Using variable-angle total internal reflection fluorescence microscopy (VA-TIRFM), structured illumination microscopy (SIM) and fluorescence cross spectroscopy (FCS), we determined that the dynamic behavior of GFP-Flot1 in Arabidopsis thaliana cotyledon epidermal cells changed significantly in plants treated with the elicitor flg22. Moreover, we found that Flot1 was constitutively recycled via an endocytic pathway and that flg22 could promote endocytosis. Importantly, targeting of Flot1 to the late endosome/vacuole for degradation increased in response to flg22 treatment; immunoblot analysis showed that when triggered by flg22, GFP-Flot1 was gradually degraded in a time-dependent manner. Taken together, these findings support the hypothesis that the changing of dynamics and oligomeric states can promote the endocytosis and degradation of Flot1 under flg22 treatment in plant cells.

Název v anglickém jazyce

The dynamics and endocytosis of Flot1 protein in response to flg22 in Arabidopsis

Popis výsledku anglicky

Membrane microdomains play vital roles in the process of bacterial infection. The membrane microdomain associated protein Flot1 acts in an endocytic pathway and is required for seedling development, however, whether Flot1 is a part of host defense mechanisms remains unknown. During an analysis of callose deposition, we found that Flot1 amiRNAi mutants exhibited defects in response to flg22. Using variable-angle total internal reflection fluorescence microscopy (VA-TIRFM), structured illumination microscopy (SIM) and fluorescence cross spectroscopy (FCS), we determined that the dynamic behavior of GFP-Flot1 in Arabidopsis thaliana cotyledon epidermal cells changed significantly in plants treated with the elicitor flg22. Moreover, we found that Flot1 was constitutively recycled via an endocytic pathway and that flg22 could promote endocytosis. Importantly, targeting of Flot1 to the late endosome/vacuole for degradation increased in response to flg22 treatment; immunoblot analysis showed that when triggered by flg22, GFP-Flot1 was gradually degraded in a time-dependent manner. Taken together, these findings support the hypothesis that the changing of dynamics and oligomeric states can promote the endocytosis and degradation of Flot1 under flg22 treatment in plant cells.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10601 - Cell biology

Projekt

<a href="/cs/project/GA16-24313S" target="_blank" >GA16-24313S: Charakterizace organizace mikrotubulů během buněčného dělení, růstu a morfogeneze rostlin pomocí superresoluční mikroskopie</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2017

Kód důvěrnosti údajů

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

Název periodika

Journal of Plant Physiology

ISSN

0176-1617

e-ISSN

—

Svazek periodika

215

Číslo periodika v rámci svazku

AUG

Stát vydavatele periodika

DE - Spolková republika Německo

Počet stran výsledku

12

Strana od-do

73-84

Kód UT WoS článku

000406651700009

EID výsledku v databázi Scopus

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