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

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Perraki, Artemis | Gronnier, Julien | Gouguet, Paul | Boudsocq, Marie | Deroubaix, Anne-Flore | Simon, Vincent | German-Retana, Sylvie | Legrand, Anthony | Habenstein, Birgit | Zipfel, Cyril | Bayer, Emmanuelle | Mongrand, Sébastien | Germain, Veronique

Edité par CCSD ; Public Library of Science -

UMR BFP - Equipe Virologie. International audience. Plants respond to pathogens through dynamic regulation of plasma membrane-bound sig-naling 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 plasmo-desmata. This study unveils plasma membrane nanodomain-associated molecular events underlying the plant immune response to viruses.

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