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REM1.3's phospho-status defines its plasma membrane nanodomain organization and activity in restricting PVX cell-to-cell movement.

Authors :
Perraki, Artemis
Gronnier, Julien
Gouguet, Paul
Boudsocq, Marie
Deroubaix, Anne-Flore
Simon, Vincent
German-Retana, Sylvie
Zipfel, Cyril
Bayer, Emmanuelle
Mongrand, Sébastien
Germain, Véronique
Legrand, Anthony
Habenstein, Birgit
Source :
PLoS Pathogens; 11/12/2018, Vol. 14 Issue 11, p1-33, 33p
Publication Year :
2018

Abstract

Plants respond to pathogens through dynamic regulation of plasma membrane-bound signaling pathways. To date, how the plant plasma membrane is involved in responses to viruses is mostly unknown. Here, we show that plant cells sense the Potato virus X (PVX) COAT PROTEIN and TRIPLE GENE BLOCK 1 proteins and subsequently trigger the activation of a membrane-bound calcium-dependent kinase. We show that the Arabidopsis thaliana CALCIUM-DEPENDENT PROTEIN KINASE 3-interacts with group 1 REMORINs in vivo, phosphorylates the intrinsically disordered N-terminal domain of the Group 1 REMORIN REM1.3, and restricts PVX cell-to-cell movement. REM1.3's phospho-status defines its plasma membrane nanodomain organization and is crucial for REM1.3-dependent restriction of PVX cell-to-cell movement by regulation of callose deposition at plasmodesmata. This study unveils plasma membrane nanodomain-associated molecular events underlying the plant immune response to viruses. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
15537366
Volume :
14
Issue :
11
Database :
Complementary Index
Journal :
PLoS Pathogens
Publication Type :
Academic Journal
Accession number :
132958540
Full Text :
https://doi.org/10.1371/journal.ppat.1007378