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Iwanishi, M, Czech, MP and Cherniack, AD (2000) The protein-tyrosine kinase fer associates with signaling complexes containing insulin receptor substrate-1 and phosphatidylinositol 3-kinase. J. Biol. Chem. 275:38995-9000


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.


PubMed Online version:10.1074/jbc.M006665200


3T3 Cells; Adipocytes/metabolism; Amino Acid Sequence; Animals; COS Cells; Cell Differentiation; Cells, Cultured; DNA, Complementary/metabolism; Electrophoresis, Polyacrylamide Gel; Gene Library; Immunoblotting; Insulin/pharmacology; Insulin Receptor Substrate Proteins; Mice; Molecular Sequence Data; Phosphatidylinositol 3-Kinases/metabolism; Phosphoproteins/metabolism; Phosphorylation; Platelet-Derived Growth Factor/pharmacology; Precipitin Tests; Protein Binding; Protein Isoforms; Protein Structure, Tertiary; Protein-Tyrosine Kinases/metabolism; Proto-Oncogene Proteins/metabolism; Recombinant Fusion Proteins/metabolism; Sequence Homology, Amino Acid; Signal Transduction; Time Factors; Transfection; Tyrosine/metabolism; src Homology Domains