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Originally published In Press as doi:10.1074/jbc.M105070200 on July 3, 2001

J. Biol. Chem., Vol. 276, Issue 36, 33361-33368, September 7, 2001
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Roles of Phosphatidylinositol 3-Kinase in Interferon-gamma -dependent Phosphorylation of STAT1 on Serine 727 and Activation of Gene Expression*

Hannah NguyenDagger , Chilakamarti V. Ramana, Joshua Bayes, and George R. Stark§

From the Department of Molecular Biology, Lerner Research Institute, The Cleveland Clinic Foundation, Cleveland, Ohio 44195

STAT1 must be phosphorylated on serine 727 to be fully active in transcription. We show that phosphatidylinositol 3-kinase (PI3K) and its effector kinase Akt play an important role in the serine phosphorylation of STAT1 and in the activation of gene expression in response to interferon-gamma (IFNgamma ). IFNgamma activates PI3K as well as Akt in a variety of cell lines. Specific inhibition of PI3K abrogates IFNgamma -induced, but not interleukin-1- or tumor necrosis factor-alpha -induced, phosphorylation of STAT1 on serine and reduces STAT1-dependent transcription and gene expression by ~7-fold. Constitutively active forms of PI3K or Akt activate and their dominant-negative derivatives inhibit STAT1-driven transactivation in response to IFNgamma . In addition to PI3K and Akt, JAK1, JAK2, and the tyrosine 440 STAT1 docking residue of IFNGR1 are required for STAT1 to be phosphorylated on serine. Taken together, these results suggest that the following events lead to the activation of STAT1 upon IFNgamma stimulation: 1) PI3K and Akt are activated by the occupied receptor and Tyr-440 is phosphorylated by the activated JAKs; 2) STAT1 docks to Tyr-440; and 3) Tyr-701 is phosphorylated by the JAKs and Ser-727 is phosphorylated by a kinase downstream of Akt.

* This work was supported in part by Grant P01 CA 62220 from the National Institutes of Health.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger Supported by a Cancer Research Institute Fellowship.

§ To whom correspondence should be addressed: Dept. of Molecular Biology, Lerner Research Inst., The Cleveland Clinic Foundation, 9500 Euclid Ave., Cleveland, OH 44195. Tel.: 216-444-3900; Fax: 216-444-3279; E-mail: starkg@ccf.org.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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