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REM1.3's phospho-status defines its plasma membrane nanodomain organization and activity in restricting PVX cell-to-cell movement.
- 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.
- Subjects :
- Arabidopsis genetics
Arabidopsis metabolism
Capsid Proteins physiology
Cell Membrane metabolism
Cell Movement
Plant Diseases virology
Plant Leaves genetics
Plant Leaves immunology
Plants, Genetically Modified virology
Plasmodesmata metabolism
Protein Kinases metabolism
Carrier Proteins metabolism
Cell Membrane immunology
Phosphoproteins metabolism
Plant Proteins metabolism
Potexvirus pathogenicity
Subjects
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