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J Biol Chem, Vol. 273, Issue 22, 13375-13378, May 29, 1998
From the Department of Biological Chemistry, University of
Michigan, Ann Arbor, Michigan 48109-0606
Phosphatidylinositol 3,4,5-trisphosphate
(PtdIns(3,4,5)P3) is a key molecule involved in cell
growth signaling. We demonstrated that overexpression of PTEN, a
putative tumor suppressor, reduced insulin-induced
PtdIns(3,4,5)P3 production in human 293 cells without
effecting insulin-induced phosphoinositide 3-kinase activation. Further, transfection of the catalytically inactive mutant of PTEN
(C124S) caused PtdIns(3,4,5)P3 accumulation in the absence of insulin stimulation. Purified recombinant PTEN catalyzed
dephosphorylation of PtdIns(3,4,5)P3, specifically at
position 3 on the inositol ring. PTEN also exhibited 3-phosphatase
activity toward inositol 1,3,4,5-tetrakisphosphate. Our results raise
the possibility that PTEN acts in vivo as a
phosphoinositide 3-phosphatase by regulating PtdIns(3,4,5)P3 levels. As expected, the C124S mutant of
PTEN was incapable of catalyzing dephosphorylation of
PtdIns(3,4,5)P3 consistent with the mechanism observed in
protein-tyrosine phosphatase-catalyzed reactions.
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