PLoS Pathogens (Nov 2018)

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

DOI
https://doi.org/10.1371/journal.ppat.1007378
Journal volume & issue
Vol. 14, no. 11
p. e1007378

Abstract

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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.