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http://purl.uniprot.org/citations/16959567http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16959567http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16959567http://www.w3.org/2000/01/rdf-schema#comment"Yersinia spp. cause gastroenteritis and the plague, representing historically devastating pathogens that are currently an important biodefense and antibiotic resistance concern. A critical virulence determinant is the Yersinia protein kinase A, or YpkA, a multidomain protein that disrupts the eukaryotic actin cytoskeleton. Here we solve the crystal structure of a YpkA-Rac1 complex and find that YpkA possesses a Rac1 binding domain that mimics host guanidine nucleotide dissociation inhibitors (GDIs) of the Rho GTPases. YpkA inhibits nucleotide exchange in Rac1 and RhoA, and mutations that disrupt the YpkA-GTPase interface abolish this activity in vitro and impair in vivo YpkA-induced cytoskeletal disruption. In cell culture experiments, the kinase and the GDI domains of YpkA act synergistically to promote cytoskeletal disruption, and a Y. pseudotuberculosis mutant lacking YpkA GDI activity shows attenuated virulence in a mouse infection assay. We conclude that virulence in Yersinia depends strongly upon mimicry of host GDI proteins by YpkA."xsd:string
http://purl.uniprot.org/citations/16959567http://purl.org/dc/terms/identifier"doi:10.1016/j.cell.2006.06.056"xsd:string
http://purl.uniprot.org/citations/16959567http://purl.org/dc/terms/identifier"doi:10.1016/j.cell.2006.06.056"xsd:string
http://purl.uniprot.org/citations/16959567http://purl.uniprot.org/core/author"Bliska J.B."xsd:string
http://purl.uniprot.org/citations/16959567http://purl.uniprot.org/core/author"Bliska J.B."xsd:string
http://purl.uniprot.org/citations/16959567http://purl.uniprot.org/core/author"Stebbins C.E."xsd:string
http://purl.uniprot.org/citations/16959567http://purl.uniprot.org/core/author"Stebbins C.E."xsd:string
http://purl.uniprot.org/citations/16959567http://purl.uniprot.org/core/author"Prehna G."xsd:string
http://purl.uniprot.org/citations/16959567http://purl.uniprot.org/core/author"Prehna G."xsd:string
http://purl.uniprot.org/citations/16959567http://purl.uniprot.org/core/author"Ivanov M.I."xsd:string
http://purl.uniprot.org/citations/16959567http://purl.uniprot.org/core/author"Ivanov M.I."xsd:string
http://purl.uniprot.org/citations/16959567http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16959567http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16959567http://purl.uniprot.org/core/name"Cell"xsd:string
http://purl.uniprot.org/citations/16959567http://purl.uniprot.org/core/name"Cell"xsd:string
http://purl.uniprot.org/citations/16959567http://purl.uniprot.org/core/pages"869-880"xsd:string
http://purl.uniprot.org/citations/16959567http://purl.uniprot.org/core/pages"869-880"xsd:string
http://purl.uniprot.org/citations/16959567http://purl.uniprot.org/core/title"Yersinia virulence depends on mimicry of host Rho-family nucleotide dissociation inhibitors."xsd:string
http://purl.uniprot.org/citations/16959567http://purl.uniprot.org/core/title"Yersinia virulence depends on mimicry of host Rho-family nucleotide dissociation inhibitors."xsd:string
http://purl.uniprot.org/citations/16959567http://purl.uniprot.org/core/volume"126"xsd:string
http://purl.uniprot.org/citations/16959567http://purl.uniprot.org/core/volume"126"xsd:string
http://purl.uniprot.org/citations/16959567http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/16959567
http://purl.uniprot.org/citations/16959567http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/16959567