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http://purl.uniprot.org/citations/18086875http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18086875http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18086875http://www.w3.org/2000/01/rdf-schema#comment"The Cdc42-like GTPase Wnt responsive Cdc42 homolog 1 (Wrch1) has several atypical features; it has an N-terminal proline-rich extension that confers binding to SH3 domains, and it harbors an extremely high intrinsic nucleotide exchange activity, which overrides the normal GTPase activity. As a result, Wrch1 resides mainly in the active, GTP-loaded conformation under normal cellular conditions. We have previously shown that ectopic expression of Wrch1 in fibroblasts resulted in an altered cell morphology visible as a formation of filopodia, a loss of stress fibers, and a reduction in focal adhesions. Here, we show that Wrch1 binds to the nonreceptor tyrosine kinase Pyk2. The interaction required Wrch1 to be in a GTP conformation and also required an intact N-terminal proline-rich extension as well as an intact effector loop. Wrch1 requires Pyk2 in imposing the cytoskeletal effects, seen as the formation of filopodia, since treatment of cells with a Pyk2-specific small interfering RNA abrogated this response. Interestingly, we found that the presence and activity of Src were needed for the formation of a Wrch1-Pyk2 complex as well as for the Wrch1-induced formation of filopodia. We propose a model in which Pyk2 and Src function to coordinate the Wrch1-dependent effects on cytoskeletal dynamics."xsd:string
http://purl.uniprot.org/citations/18086875http://purl.org/dc/terms/identifier"doi:10.1128/mcb.00201-07"xsd:string
http://purl.uniprot.org/citations/18086875http://purl.org/dc/terms/identifier"doi:10.1128/mcb.00201-07"xsd:string
http://purl.uniprot.org/citations/18086875http://purl.uniprot.org/core/author"Aspenstrom P."xsd:string
http://purl.uniprot.org/citations/18086875http://purl.uniprot.org/core/author"Aspenstrom P."xsd:string
http://purl.uniprot.org/citations/18086875http://purl.uniprot.org/core/author"Ruusala A."xsd:string
http://purl.uniprot.org/citations/18086875http://purl.uniprot.org/core/author"Ruusala A."xsd:string
http://purl.uniprot.org/citations/18086875http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18086875http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18086875http://purl.uniprot.org/core/name"Mol. Cell. Biol."xsd:string
http://purl.uniprot.org/citations/18086875http://purl.uniprot.org/core/name"Mol. Cell. Biol."xsd:string
http://purl.uniprot.org/citations/18086875http://purl.uniprot.org/core/pages"1802-1814"xsd:string
http://purl.uniprot.org/citations/18086875http://purl.uniprot.org/core/pages"1802-1814"xsd:string
http://purl.uniprot.org/citations/18086875http://purl.uniprot.org/core/title"The atypical Rho GTPase Wrch1 collaborates with the nonreceptor tyrosine kinases Pyk2 and Src in regulating cytoskeletal dynamics."xsd:string
http://purl.uniprot.org/citations/18086875http://purl.uniprot.org/core/title"The atypical Rho GTPase Wrch1 collaborates with the nonreceptor tyrosine kinases Pyk2 and Src in regulating cytoskeletal dynamics."xsd:string
http://purl.uniprot.org/citations/18086875http://purl.uniprot.org/core/volume"28"xsd:string
http://purl.uniprot.org/citations/18086875http://purl.uniprot.org/core/volume"28"xsd:string
http://purl.uniprot.org/citations/18086875http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/18086875
http://purl.uniprot.org/citations/18086875http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/18086875
http://purl.uniprot.org/citations/18086875http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/18086875
http://purl.uniprot.org/citations/18086875http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/18086875
http://purl.uniprot.org/uniprot/Q14289http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/18086875
http://purl.uniprot.org/uniprot/Q7L0Q8http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/18086875