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Direct Regulation of the Akt Proto-Oncogene Product By Phosphatidylinosital-3,4-Bisphosphate

  1. Author:
    Franke, T. F.
    Kaplan, D. R.
    Cantley, L. C.
    Toker, A.

  2. Author Address

    Franke TF NCI ABL BASIC RES PROGRAM FREDERICK CANC RES FACIL & DEV CTR FREDERICK, MD 21702 USA MCGILL UNIV MONTREAL NEUROL INST MONTREAL PQ H3A 2B4 CANADA HARVARD UNIV BETH ISRAEL HOSP SCH MED DEPT CELL BIOL DIV SIGNAL TRANSDUCTION BOSTON, MA 02115 USA
    1. Year: 1997
  2. Journal: Science
    1. 275
    2. 5300
    3. Pages: 665-668
  4. Type of Article: Article
  1. Abstract:

    The regulation of the serine-threonine kinase Akt by lipid products of phosphoinositide 3-kinase (PI 3-kinase) was investigated. Akt activity was found to correlate with the amount of phosphatidylinositol-3,4-bisphosphate (PtdIns-3,4-P-2) in vivo, and synthetic PtdIns-3,4-P-2 activated Akt both in vitro and in vivo. Binding of PtdIns-3,4-P-2 occurred within the Akt pleckstrin homology (PH) domain and facilitated dimerization of Akt. Akt mutated in the PH domain was not activated by PI 3-kinase in vivo or by PtdIns-3,4-P-2 in vitro, and it was impaired in binding to PtdIns-3,4-P-2. Examination of the binding to other phosphoinositides revealed that they bound to the Akt PH domain with much lower affinity than did PtdIns-3,4-P-2 and failed to increase Akt activity. Thus, Akt is apparently regulated by the direct interaction of PtdIns-3,4-P-2 with the Akt PH domain. [References: 18]

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