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http://purl.uniprot.org/citations/18996344http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18996344http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18996344http://www.w3.org/2000/01/rdf-schema#comment"The Salmonella typhimurium type III secretion effector protein SifA is essential for inducing tubulation of the Salmonella phagosome and binds the mammalian kinesin-binding protein SKIP. Coexpression of SifA with the effector SseJ induced tubulation of mammalian cell endosomes, similar to that induced by Salmonella infection. Interestingly, GTP-bound RhoA, RhoB, and RhoC also induced endosomal tubulation when coexpressed with SseJ, indicating that SifA likely mimics or activates a RhoA family GTPase. The structure of SifA in complex with the PH domain of SKIP revealed that SifA has two distinct domains; the amino terminus binds SKIP, and the carboxyl terminus has a fold similar to SopE, a Salmonella effector with Rho GTPase guanine nucleotide exchange factor activity (GEF). Similar to GEFs, SifA interacted with GDP-bound RhoA, and purified SseJ and RhoA formed a protein complex, suggesting that SifA, SKIP, SseJ, and RhoA family GTPases cooperatively promote host membrane tubulation."xsd:string
http://purl.uniprot.org/citations/18996344http://purl.org/dc/terms/identifier"doi:10.1016/j.chom.2008.08.012"xsd:string
http://purl.uniprot.org/citations/18996344http://purl.org/dc/terms/identifier"doi:10.1016/j.chom.2008.08.012"xsd:string
http://purl.uniprot.org/citations/18996344http://purl.uniprot.org/core/author"Miller S.I."xsd:string
http://purl.uniprot.org/citations/18996344http://purl.uniprot.org/core/author"Miller S.I."xsd:string
http://purl.uniprot.org/citations/18996344http://purl.uniprot.org/core/author"Huang Z."xsd:string
http://purl.uniprot.org/citations/18996344http://purl.uniprot.org/core/author"Huang Z."xsd:string
http://purl.uniprot.org/citations/18996344http://purl.uniprot.org/core/author"Dixon J.E."xsd:string
http://purl.uniprot.org/citations/18996344http://purl.uniprot.org/core/author"Dixon J.E."xsd:string
http://purl.uniprot.org/citations/18996344http://purl.uniprot.org/core/author"Chai J."xsd:string
http://purl.uniprot.org/citations/18996344http://purl.uniprot.org/core/author"Chai J."xsd:string
http://purl.uniprot.org/citations/18996344http://purl.uniprot.org/core/author"Alto N.M."xsd:string
http://purl.uniprot.org/citations/18996344http://purl.uniprot.org/core/author"Alto N.M."xsd:string
http://purl.uniprot.org/citations/18996344http://purl.uniprot.org/core/author"Blanc M.-P."xsd:string
http://purl.uniprot.org/citations/18996344http://purl.uniprot.org/core/author"Blanc M.-P."xsd:string
http://purl.uniprot.org/citations/18996344http://purl.uniprot.org/core/author"Ohlson M.B."xsd:string
http://purl.uniprot.org/citations/18996344http://purl.uniprot.org/core/author"Ohlson M.B."xsd:string
http://purl.uniprot.org/citations/18996344http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18996344http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18996344http://purl.uniprot.org/core/name"Cell Host Microbe"xsd:string
http://purl.uniprot.org/citations/18996344http://purl.uniprot.org/core/name"Cell Host Microbe"xsd:string
http://purl.uniprot.org/citations/18996344http://purl.uniprot.org/core/pages"434-446"xsd:string
http://purl.uniprot.org/citations/18996344http://purl.uniprot.org/core/pages"434-446"xsd:string