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http://purl.uniprot.org/citations/21926430http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21926430http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21926430http://www.w3.org/2000/01/rdf-schema#comment"Sorting nexin 27 (SNX27) is a 62-kDa protein localized to early endosomes and known to regulate the intracellular trafficking of ion channels and receptors. In addition to a PX domain, SNX27 is the only sorting family member that contains a PDZ domain. To identify novel SNX27-PDZ binding partners, we performed a proteomic screen in mouse principal kidney cortical collecting duct cells using a GST-SNX27 fusion construct as bait. We found that β-Pix (p21-activated kinase-interactive exchange factor), a guanine nucleotide exchange factor for the Rho family of small GTPases known to regulate cell motility directly interacted with SNX27. The association of β-Pix and SNX27 is specific for β-Pix isoforms terminating in the type-1 PDZ binding motif (ETNL). In the same screen we also identified Git1/2 as a potential SNX27 interacting protein. The interaction between SNX27 and Git1/2 is indirect and mediated by β-Pix. Furthermore, we show recruitment of the β-Pix·Git complex to endosomal sites in a SNX27-dependent manner. Finally, migration assays revealed that depletion of SNX27 from HeLa and mouse principal kidney cortical collecting duct cells significantly decreases cell motility. We propose a model by which SNX27 regulates trafficking of β-Pix to focal adhesions and thereby influences cell motility."xsd:string
http://purl.uniprot.org/citations/21926430http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m111.260802"xsd:string
http://purl.uniprot.org/citations/21926430http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m111.260802"xsd:string
http://purl.uniprot.org/citations/21926430http://purl.uniprot.org/core/author"Tang J."xsd:string
http://purl.uniprot.org/citations/21926430http://purl.uniprot.org/core/author"Tang J."xsd:string
http://purl.uniprot.org/citations/21926430http://purl.uniprot.org/core/author"Milgram S.L."xsd:string
http://purl.uniprot.org/citations/21926430http://purl.uniprot.org/core/author"Milgram S.L."xsd:string
http://purl.uniprot.org/citations/21926430http://purl.uniprot.org/core/author"Kuo J.C."xsd:string
http://purl.uniprot.org/citations/21926430http://purl.uniprot.org/core/author"Kuo J.C."xsd:string
http://purl.uniprot.org/citations/21926430http://purl.uniprot.org/core/author"McDermott M.I."xsd:string
http://purl.uniprot.org/citations/21926430http://purl.uniprot.org/core/author"McDermott M.I."xsd:string
http://purl.uniprot.org/citations/21926430http://purl.uniprot.org/core/author"Playford M.P."xsd:string
http://purl.uniprot.org/citations/21926430http://purl.uniprot.org/core/author"Playford M.P."xsd:string
http://purl.uniprot.org/citations/21926430http://purl.uniprot.org/core/author"Valdes J.L."xsd:string
http://purl.uniprot.org/citations/21926430http://purl.uniprot.org/core/author"Valdes J.L."xsd:string
http://purl.uniprot.org/citations/21926430http://purl.uniprot.org/core/author"Waterman C.M."xsd:string
http://purl.uniprot.org/citations/21926430http://purl.uniprot.org/core/author"Waterman C.M."xsd:string
http://purl.uniprot.org/citations/21926430http://purl.uniprot.org/core/author"Wincovitch S.M."xsd:string
http://purl.uniprot.org/citations/21926430http://purl.uniprot.org/core/author"Wincovitch S.M."xsd:string
http://purl.uniprot.org/citations/21926430http://purl.uniprot.org/core/author"Zimmerman S.P."xsd:string
http://purl.uniprot.org/citations/21926430http://purl.uniprot.org/core/author"Zimmerman S.P."xsd:string
http://purl.uniprot.org/citations/21926430http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/21926430http://purl.uniprot.org/core/date"2011"xsd:gYear