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

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, Véronique Germain

Research output: Contribution to journalArticlepeer-review

29 Citations (Scopus)
6 Downloads (Pure)

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.
Original languageEnglish
Article numbere1007378
JournalPLoS Pathogens
Volume14
Issue number11
DOIs
Publication statusPublished - 12 Nov 2018

Cite this