Akt-2 Binds to Glut4-containing Vesicles and Phosphorylates Their Component Proteins in Response to Insulin

• Published in: The Journal of biological chemistry Vol. 274; no. 3; pp. 1458 - 1464
• Main Authors: Kupriyanova, T A, Kandror, K V
• Format: Journal Article
• Language: English
• Published: United States American Society for Biochemistry and Molecular Biology 15.01.1999
• Subjects: Adipocytes - drug effects; Adipocytes - metabolism; Androstadienes - pharmacology; Animals; Blotting, Western; Chromatography, Ion Exchange; Enzyme Activation; Glucose Transporter Type 4; Insulin - pharmacology; Insulin Antagonists - pharmacology; Male; Monosaccharide Transport Proteins - metabolism; Muscle Proteins; Phosphorylation; Protein-Serine-Threonine Kinases; Protein-Tyrosine Kinases - metabolism; Proto-Oncogene Proteins - metabolism; Proto-Oncogene Proteins c-akt; Rats; Rats, Sprague-Dawley; Signal Transduction; Substrate Specificity; Wortmannin
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1074/jbc.274.3.1458

Glut4-containing vesicles immunoadsorbed from primary rat adipocytes possess endogenous protein kinase activity and phosphorylation substrates. Phosphorylation of several vesicle proteins including Glut4 itself is rapidly activated by insulin. Wortmannin blocks the effect of insulin when added to cells in vivo prior to insulin administration. By means of MonoQ chromatography and Western blot analysis, vesicle-associated protein kinase is identified as Akt-2, a lipid-binding protein kinase involved in insulin signaling. Akt-2 is found to be recruited to Glut4-containing vesicles in response to insulin.