GONUTS has been updated to MW1.31 Most things seem to be working but be sure to report problems.

Have any questions? Please email us at ecoliwiki@gmail.com

TableEdit

Jump to: navigation, search

PMID:11006284

You don't have sufficient rights on this wiki to edit tables. Perhaps you need to log in. Changes you make in the Table editor will not be saved back to the wiki

See Help for Help on this wiki. See the documentation for how to use the table editor

Citation

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

Abstract

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.

Links

PubMed Online version:10.1074/jbc.M006665200

Keywords

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

public



Cancel