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

Authors :
Perraki A
Gronnier J
Gouguet P
Boudsocq M
Deroubaix AF
Simon V
German-Retana S
Legrand A
Habenstein B
Zipfel C
Bayer E
Mongrand S
Germain V
Source :
PLoS pathogens [PLoS Pathog] 2018 Nov 12; Vol. 14 (11), pp. e1007378. Date of Electronic Publication: 2018 Nov 12 (Print Publication: 2018).
Publication Year :
2018

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.<br />Competing Interests: The authors have declared that no competing interests exist.

Details

Language :
English
ISSN :
1553-7374
Volume :
14
Issue :
11
Database :
MEDLINE
Journal :
PLoS pathogens
Publication Type :
Academic Journal
Accession number :
30419072
Full Text :
https://doi.org/10.1371/journal.ppat.1007378