Akt (PKB, Rac kinase) is a 60kDa ser/thr kinase critical for controlling diverse cellular functions, including glucose metabolism, gene transcription, cell proliferation, and apoptosis. Akt phosphorylates a number of substrates including MBP, glycogen synthetase, PKA RII subunit, and histone H1. Akt is activated in response to insulin and growth factors in a PI3-kinase dependent manner. Activation of PI3-Kinase generates phosphatidylinositol 3,4-bisphosphate, which induces membrane translocation of Akt coincident with its phosphorylation at Thr-308 and Ser-473. Upon activation, Akt associates with members of the PKC family of kinases, such as PKCdelta and PKCzeta. Ceramide-activated PKCzeta leads to phosphorylation of Thr-34 within the pleckstrin homology domain of Akt. This phosphorylation inhibits PIP3 binding to Akt preventing activation of the kinase and may lead to cermide-induced cell death.
Akt (PKB, Rac kinase) is a 60kDa ser/thr kinase critical for controlling diverse cellular functions, including glucose metabolism, gene transcription, cell proliferation, and apoptosis. Akt phosphorylates a number of substrates including MBP, glycogen syn
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