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http://purl.uniprot.org/citations/17420256http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17420256http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17420256http://www.w3.org/2000/01/rdf-schema#comment"M-CSF is known to induce cytoskeletal reorganization in macrophages and osteoclasts by activation of phosphatidylinositol 3-kinase (PI3K) and c-Src, but the detailed mechanisms remain unclear. We find, unexpectedly, that tyrosine (Tyr) to phenylalanine (Phe) mutation of Tyr-721, the PI3K binding site in the M-CSF receptor c-Fms, fails to suppress cytoskeletal remodeling or actin ring formation. In contrast, mutation of c-Fms Tyr-559 to Phe blocks M-CSF-induced cytoskeletal reorganization by inhibiting formation of a Src Family Kinase SFK.c-Cbl.PI3K complex and the downstream activation of Vav3 and Rac, two key mediators of actin remodeling. Using an add-back approach in which specific Tyr residues are reinserted into c-Fms inactivated by the absence of all seven functionally important Tyr residues, we find that Tyr-559 is necessary but not sufficient to transduce M-CSF-dependent cytoskeletal reorganization. Furthermore, this same add-back approach identifies important roles for Tyr-697 and Tyr-721 in collaborating with Tyr-559 to recruit a multimeric signaling complex that can transduce signals from c-Fms to the actin cytoskeleton."xsd:string
http://purl.uniprot.org/citations/17420256http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m610937200"xsd:string
http://purl.uniprot.org/citations/17420256http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m610937200"xsd:string
http://purl.uniprot.org/citations/17420256http://purl.uniprot.org/core/author"Takeshita S."xsd:string
http://purl.uniprot.org/citations/17420256http://purl.uniprot.org/core/author"Takeshita S."xsd:string
http://purl.uniprot.org/citations/17420256http://purl.uniprot.org/core/author"Ross F.P."xsd:string
http://purl.uniprot.org/citations/17420256http://purl.uniprot.org/core/author"Ross F.P."xsd:string
http://purl.uniprot.org/citations/17420256http://purl.uniprot.org/core/author"Teitelbaum S.L."xsd:string
http://purl.uniprot.org/citations/17420256http://purl.uniprot.org/core/author"Teitelbaum S.L."xsd:string
http://purl.uniprot.org/citations/17420256http://purl.uniprot.org/core/author"Chappel J."xsd:string
http://purl.uniprot.org/citations/17420256http://purl.uniprot.org/core/author"Chappel J."xsd:string
http://purl.uniprot.org/citations/17420256http://purl.uniprot.org/core/author"Colaianni G."xsd:string
http://purl.uniprot.org/citations/17420256http://purl.uniprot.org/core/author"Colaianni G."xsd:string
http://purl.uniprot.org/citations/17420256http://purl.uniprot.org/core/author"Faccio R."xsd:string
http://purl.uniprot.org/citations/17420256http://purl.uniprot.org/core/author"Faccio R."xsd:string
http://purl.uniprot.org/citations/17420256http://purl.uniprot.org/core/author"Zallone A."xsd:string
http://purl.uniprot.org/citations/17420256http://purl.uniprot.org/core/author"Zallone A."xsd:string
http://purl.uniprot.org/citations/17420256http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17420256http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17420256http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/17420256http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/17420256http://purl.uniprot.org/core/pages"18991-18999"xsd:string
http://purl.uniprot.org/citations/17420256http://purl.uniprot.org/core/pages"18991-18999"xsd:string