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

hal.structure.identifierLaboratoire de biogenèse membranaire [LBM]
dc.contributor.authorPERRAKI, Artemis
hal.structure.identifierLaboratoire de biogenèse membranaire [LBM]
dc.contributor.authorGRONNIER, Julien
hal.structure.identifierLaboratoire de biogenèse membranaire [LBM]
dc.contributor.authorGOUGUET, Paul
hal.structure.identifierInstitut des Sciences des Plantes de Paris-Saclay [IPS2 (UMR_9213 / UMR_1403)]
dc.contributor.authorBOUDSOCQ, Marie
hal.structure.identifierLaboratoire de biogenèse membranaire [LBM]
dc.contributor.authorDEROUBAIX, Anne-Flore
hal.structure.identifierBiologie du fruit et pathologie [BFP]
dc.contributor.authorSIMON, Vincent
hal.structure.identifierBiologie du fruit et pathologie [BFP]
dc.contributor.authorGERMAN-RETANA, Sylvie
hal.structure.identifierLaboratoire de biogenèse membranaire [LBM]
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorLEGRAND, Anthony
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorHABENSTEIN, Birgit
hal.structure.identifierUniversität Zürich [Zürich] = University of Zurich [UZH]
dc.contributor.authorZIPFEL, Cyril
hal.structure.identifierLaboratoire de biogenèse membranaire [LBM]
dc.contributor.authorBAYER, Emmanuelle
hal.structure.identifierLaboratoire de biogenèse membranaire [LBM]
dc.contributor.authorMONGRAND, Sébastien
hal.structure.identifierBiologie du fruit et pathologie [BFP]
dc.contributor.authorGERMAIN, Veronique
dc.date.issued2018
dc.identifier.issn1553-7366
dc.description.abstractEnPlants respond to pathogens through dynamic regulation of plasma membrane-bound sig-naling 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 plasmo-desmata. This study unveils plasma membrane nanodomain-associated molecular events underlying the plant immune response to viruses.
dc.description.sponsorshipFacteurs cellulaires recrutés par les potyvirus pour leur transport intercellulaire : de nouvelles sources de résistance des plantes?
dc.description.sponsorshipSaclay Plant Sciences
dc.language.isoen
dc.publisherPublic Library of Science
dc.rights.urihttp://creativecommons.org/licenses/by/
dc.title.enREM1.3's phospho-status defines its plasma membrane nanodomain organization and activity in restricting PVX cell-to-cell movement
dc.typeArticle de revue
dc.identifier.doi10.1371/journal.ppat.1007378
dc.subject.halSciences du Vivant [q-bio]/Biologie végétale/Phytopathologie et phytopharmacie
dc.subject.halSciences du Vivant [q-bio]/Immunologie
dc.description.sponsorshipEuropeSignaling initiation and specificity in BAK1-dependent receptor kinase-mediated innate immunity in Arabidopsis
bordeaux.journalPLoS Pathogens
bordeaux.pagee1007378
bordeaux.volume14
bordeaux.issue11
bordeaux.peerReviewedoui
hal.identifierhal-02159426
hal.version1
hal.popularnon
hal.audienceInternationale
hal.origin.linkhttps://hal.archives-ouvertes.fr//hal-02159426v1
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