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. 1997 Jul 25;277(5325):567-70.
doi: 10.1126/science.277.5325.567.

Dual role of phosphatidylinositol-3,4,5-trisphosphate in the activation of protein kinase B

D Stokoe  1 , L R Stephens, T Copeland, P R Gaffney, C B Reese, G F Painter, A B Holmes, F McCormick, P T Hawkins
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Dual role of phosphatidylinositol-3,4,5-trisphosphate in the activation of protein kinase B

D Stokoe et al. Science. .

Abstract

Protein kinase B (PKB) is a proto-oncogene that is activated in signaling pathways initiated by phosphoinositide 3-kinase. Chromatographic separation of brain cytosol revealed a kinase activity that phosphorylated and activated PKB only in the presence of phosphatidylinositol-3,4,5-trisphosphate [PtdIns(3,4,5)P3]. Phosphorylation occurred exclusively on threonine-308, a residue implicated in activation of PKB in vivo. PtdIns(3,4,5)P3 was determined to have a dual role: Its binding to the pleckstrin homology domain of PKB was required to allow phosphorylation by the upstream kinase and it directly activated the upstream kinase.

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