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http://purl.uniprot.org/citations/15561106http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15561106http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15561106http://www.w3.org/2000/01/rdf-schema#comment"Fgr participates in integrin signaling in myeloid leukocytes. To examine the role of its specific domains in regulating cell migration, we expressed various Fgr molecules in COS-7 cells. Full-length, membrane-bound Fgr, but not an N-terminal truncation mutant that distributed to an intracellular compartment, increased cell migration on fibronectin and enhanced phosphorylation of the p85 subunit of phosphatidylinositol 3-kinase (PI3K), cortactin and focal adhesion kinase (FAK) at Y397 and Y576. Fgr increased Rac GTP loading, and phosphorylation of the Rac GEF Vav2, and bound to a protein complex formed by the Rho inhibitor p190RhoGAP and FAK, increasing p190RhoGAP phosphorylation, in a manner absolutely dependent on membrane localization. A kinase-defective truncation mutant of Fgr increased cell migration, albeit to a much lower extent than full-length Fgr, and was found to associate with the plasma membrane, to activate Rac and to form complexes with p190RhoGAP/FAK. Formation of complexes between p190RhoGAP, Fgr, and the FAK-related protein Pyk2 were also detected in murine macrophages. These findings suggest that the proto-oncogene Fgr regulates cell migration impinging on a signaling pathway implicating FAK/Pyk2 and leading to activation of Rac and the Rho inhibitor p190RhoGAP."xsd:string
http://purl.uniprot.org/citations/15561106http://purl.org/dc/terms/identifier"doi:10.1016/j.yexcr.2004.09.005"xsd:string
http://purl.uniprot.org/citations/15561106http://purl.org/dc/terms/identifier"doi:10.1016/j.yexcr.2004.09.005"xsd:string
http://purl.uniprot.org/citations/15561106http://purl.uniprot.org/core/author"Baruzzi A."xsd:string
http://purl.uniprot.org/citations/15561106http://purl.uniprot.org/core/author"Baruzzi A."xsd:string
http://purl.uniprot.org/citations/15561106http://purl.uniprot.org/core/author"Berton G."xsd:string
http://purl.uniprot.org/citations/15561106http://purl.uniprot.org/core/author"Berton G."xsd:string
http://purl.uniprot.org/citations/15561106http://purl.uniprot.org/core/author"Lowell C.A."xsd:string
http://purl.uniprot.org/citations/15561106http://purl.uniprot.org/core/author"Lowell C.A."xsd:string
http://purl.uniprot.org/citations/15561106http://purl.uniprot.org/core/author"Fumagalli L."xsd:string
http://purl.uniprot.org/citations/15561106http://purl.uniprot.org/core/author"Fumagalli L."xsd:string
http://purl.uniprot.org/citations/15561106http://purl.uniprot.org/core/author"Caveggion E."xsd:string
http://purl.uniprot.org/citations/15561106http://purl.uniprot.org/core/author"Caveggion E."xsd:string
http://purl.uniprot.org/citations/15561106http://purl.uniprot.org/core/author"Continolo S."xsd:string
http://purl.uniprot.org/citations/15561106http://purl.uniprot.org/core/author"Continolo S."xsd:string
http://purl.uniprot.org/citations/15561106http://purl.uniprot.org/core/author"Majeed M."xsd:string
http://purl.uniprot.org/citations/15561106http://purl.uniprot.org/core/author"Majeed M."xsd:string
http://purl.uniprot.org/citations/15561106http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/15561106http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/15561106http://purl.uniprot.org/core/name"Exp. Cell Res."xsd:string
http://purl.uniprot.org/citations/15561106http://purl.uniprot.org/core/name"Exp. Cell Res."xsd:string
http://purl.uniprot.org/citations/15561106http://purl.uniprot.org/core/pages"253-269"xsd:string
http://purl.uniprot.org/citations/15561106http://purl.uniprot.org/core/pages"253-269"xsd:string