RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/30419072http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/30419072http://www.w3.org/2000/01/rdf-schema#comment"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."xsd:string
http://purl.uniprot.org/citations/30419072http://purl.org/dc/terms/identifier"doi:10.1371/journal.ppat.1007378"xsd:string
http://purl.uniprot.org/citations/30419072http://purl.uniprot.org/core/author"Zipfel C."xsd:string
http://purl.uniprot.org/citations/30419072http://purl.uniprot.org/core/author"Germain V."xsd:string
http://purl.uniprot.org/citations/30419072http://purl.uniprot.org/core/author"Mongrand S."xsd:string
http://purl.uniprot.org/citations/30419072http://purl.uniprot.org/core/author"Simon V."xsd:string
http://purl.uniprot.org/citations/30419072http://purl.uniprot.org/core/author"Bayer E."xsd:string
http://purl.uniprot.org/citations/30419072http://purl.uniprot.org/core/author"German-Retana S."xsd:string
http://purl.uniprot.org/citations/30419072http://purl.uniprot.org/core/author"Legrand A."xsd:string
http://purl.uniprot.org/citations/30419072http://purl.uniprot.org/core/author"Boudsocq M."xsd:string
http://purl.uniprot.org/citations/30419072http://purl.uniprot.org/core/author"Habenstein B."xsd:string
http://purl.uniprot.org/citations/30419072http://purl.uniprot.org/core/author"Perraki A."xsd:string
http://purl.uniprot.org/citations/30419072http://purl.uniprot.org/core/author"Gouguet P."xsd:string
http://purl.uniprot.org/citations/30419072http://purl.uniprot.org/core/author"Gronnier J."xsd:string
http://purl.uniprot.org/citations/30419072http://purl.uniprot.org/core/author"Deroubaix A.F."xsd:string
http://purl.uniprot.org/citations/30419072http://purl.uniprot.org/core/date"2018"xsd:gYear
http://purl.uniprot.org/citations/30419072http://purl.uniprot.org/core/name"PLoS Pathog"xsd:string
http://purl.uniprot.org/citations/30419072http://purl.uniprot.org/core/pages"e1007378"xsd:string
http://purl.uniprot.org/citations/30419072http://purl.uniprot.org/core/title"REM1.3's phospho-status defines its plasma membrane nanodomain organization and activity in restricting PVX cell-to-cell movement."xsd:string
http://purl.uniprot.org/citations/30419072http://purl.uniprot.org/core/volume"14"xsd:string
http://purl.uniprot.org/citations/30419072http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/30419072
http://purl.uniprot.org/citations/30419072http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/30419072
http://purl.uniprot.org/uniprot/#_O80837-mappedCitation-30419072http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/30419072
http://purl.uniprot.org/uniprot/#_Q42479-mappedCitation-30419072http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/30419072