Open AccessREM1.3's phospho-status defines its plasma membrane nanodomain organization and activity in restricting PVX cell-to-cell movement
Author(s) -
Artemis Perraki,
Julien Gronnier,
Paul Gouguet,
Marie Boudsocq,
Anne-Flore Deroubaix,
Vincent Simon,
Sylvie German-Retana,
Anthony Legrand,
Birgit Habenstein,
Cyril Zipfel,
Emmanuelle Bayer,
Sébastien Mongrand,
V. Germain
Publication year - 2018
Publication title -
plos pathogens
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.719
H-Index - 206
eISSN - 1553-7374
pISSN - 1553-7366
DOI - 10.1371/journal.ppat.1007378
Subject(s) - plasmodesma , microbiology and biotechnology , callose , biology , potato virus x , arabidopsis thaliana , cell membrane , cell , cell wall , biochemistry , gene , rna , cytoplasm , mutant
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.