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http://purl.uniprot.org/citations/11006284http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11006284http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11006284http://www.w3.org/2000/01/rdf-schema#comment"In a screen for 3T3-F442A adipocyte proteins that bind SH2 domains, we isolated a cDNA encoding Fer, a nonreceptor protein-tyrosine kinase of the Fes/Fps family that contains a functional SH2 domain. A truncated splicing variant, iFer, was also cloned. iFer is devoid of both the tyrosine kinase domain and a functional SH2 domain but displays a unique 42-residue C terminus and retains the ability to form oligomers with Fer. Expression of both Fer and iFer proteins are strikingly increased upon differentiation of 3T3-L1 fibroblasts to adipocytes. Platelet-derived growth factor treatment of the cultured adipocytes caused rapid tyrosine phosphorylation of Fer and its recruitment to complexes containing platelet-derived growth factor receptor and the p85 regulatory subunit of phosphatidylinositol (PI) 3-kinase. Insulin treatment of 3T3-L1 adipocytes stimulated association of Fer with complexes containing tyrosine phosphorylated IRS-1 and PI 3-kinase but did not stimulate tyrosine phosphorylation of Fer. PI 3-kinase activity in anti-Fer immunoprecipitates was also acutely activated by insulin treatment of cultured adipocytes. These data demonstrate the presence of Fer tyrosine kinase in insulin signaling complexes, suggesting a role of Fer in insulin action."xsd:string
http://purl.uniprot.org/citations/11006284http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m006665200"xsd:string
http://purl.uniprot.org/citations/11006284http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m006665200"xsd:string
http://purl.uniprot.org/citations/11006284http://purl.uniprot.org/core/author"Czech M.P."xsd:string
http://purl.uniprot.org/citations/11006284http://purl.uniprot.org/core/author"Czech M.P."xsd:string
http://purl.uniprot.org/citations/11006284http://purl.uniprot.org/core/author"Cherniack A.D."xsd:string
http://purl.uniprot.org/citations/11006284http://purl.uniprot.org/core/author"Cherniack A.D."xsd:string
http://purl.uniprot.org/citations/11006284http://purl.uniprot.org/core/author"Iwanishi M."xsd:string
http://purl.uniprot.org/citations/11006284http://purl.uniprot.org/core/author"Iwanishi M."xsd:string
http://purl.uniprot.org/citations/11006284http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/11006284http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/11006284http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/11006284http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/11006284http://purl.uniprot.org/core/pages"38995-39000"xsd:string
http://purl.uniprot.org/citations/11006284http://purl.uniprot.org/core/pages"38995-39000"xsd:string
http://purl.uniprot.org/citations/11006284http://purl.uniprot.org/core/title"The protein-tyrosine kinase fer associates with signaling complexes containing insulin receptor substrate-1 and phosphatidylinositol 3-kinase."xsd:string
http://purl.uniprot.org/citations/11006284http://purl.uniprot.org/core/title"The protein-tyrosine kinase fer associates with signaling complexes containing insulin receptor substrate-1 and phosphatidylinositol 3-kinase."xsd:string
http://purl.uniprot.org/citations/11006284http://purl.uniprot.org/core/volume"275"xsd:string
http://purl.uniprot.org/citations/11006284http://purl.uniprot.org/core/volume"275"xsd:string
http://purl.uniprot.org/citations/11006284http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11006284
http://purl.uniprot.org/citations/11006284http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11006284
http://purl.uniprot.org/citations/11006284http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/11006284
http://purl.uniprot.org/citations/11006284http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/11006284