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    J Biol Chem. 2006 Sep 29;281(39):29174-80. Epub 2006 Jul 31.

    A role for 14-3-3 in insulin-stimulated GLUT4 translocation through its interaction with the RabGAP AS160.

    Ramm G, Larance M, Guilhaus M, James DE.

    Source

    Diabetes and Obesity Program, Garvan Institute of Medical Research, Sydney, NSW, Australia. g.ramm@garvan.org.au

    Abstract

    Translocation of the insulin-regulated glucose transporter GLUT4 to the cell surface is dependent on the phosphatidylinositol 3-kinase/Akt pathway. The RabGAP (Rab GTPase-activating protein) AS160 (Akt substrate of 160 kDa) is a direct substrate of Akt and plays an essential role in the regulation of GLUT4 trafficking. We have used liquid chromatography tandem mass spectrometry to identify several 14-3-3 isoforms as AS160-interacting proteins. 14-3-3 proteins interact with AS160 in an insulin- and Akt-dependent manner via an Akt phosphorylation site, Thr-642. This correlates with the dominant negative effect of both the AS160(T642A) and the AS160(4P) mutants on insulin-stimulated GLUT4 translocation. Introduction of a constitutive 14-3-3 binding site into AS160(4P) restored 14-3-3 binding without disrupting AS160-IRAP (insulin-responsive amino peptidase) interaction and reversed the inhibitory effect of AS160(4P) on GLUT4 translocation. These data show that the insulin-dependent association of 14-3-3 with AS160 plays an important role in GLUT4 trafficking in adipocytes.

    PMID:
    16880201
    [PubMed - indexed for MEDLINE]
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