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    Biochem Biophys Res Commun. 2008 Dec 12;377(2):679-84. Epub 2008 Oct 21.

    Galphaq reduces cAMP production by decreasing Galphas protein abundance.

    Tang T, Gao MH, Miyanohara A, Hammond HK.

    Source

    Department of Medicine , University of California San Diego, La Jolla, California 92039, USA.

    Abstract

    The heterotrimeric guanine nucleotide-binding protein Galphaq transduces signals from heptahelical transmembrane receptors (e.g., alpha(1)-adrenergic, endothelin 1A, and angiotensin II) to stimulate generation of inositol-1,4,5-trisphosphate and diacylglycerol. In addition, Galphaq decreases cAMP production, through unknown mechanisms, and thus affects physiological responsiveness of cardiac myocytes and other cells. Here, we provide evidence that Galphaq expression increases Galphas ubiquitination, decreases Galphas protein content, and impairs basal and beta(1)-adrenergic receptor-stimulated cAMP production. These biochemical and functional changes are associated with Akt activation. Expression of constitutively active Akt also decreases Galphas protein content and inhibits basal and beta(1)-adrenergic receptor-stimulated cAMP production. Akt knockdown inhibits Galphaq-induced reduction of Galphas protein. In addition, MDM2, an E3 ubiquitin ligase, binds Galphas and promotes its degradation. Therefore, increased expression of Galphaq decreases cAMP production through Akt-mediated Galphas protein ubiquitination and proteasomal degradation.

    PMID:
    18948082
    [PubMed - indexed for MEDLINE]
    PMCID:
    PMC2688725
    Free PMC Article

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