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

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 and Germain, Véronique (2018) REM1.3's phospho-status defines its plasma membrane nanodomain organization and activity in restricting PVX cell-to-cell movement. PLoS Pathogens, 14 (11). ISSN 1553-7374

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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.

Item Type: Article
Faculty \ School: Faculty of Science > The Sainsbury Laboratory
UEA Research Groups: Faculty of Science > Research Groups > Plant Sciences
Depositing User: LivePure Connector
Date Deposited: 30 Jan 2019 15:31
Last Modified: 22 Oct 2022 04:26
URI: https://ueaeprints.uea.ac.uk/id/eprint/69750
DOI: 10.1371/journal.ppat.1007378

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