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Originally published In Press as doi:10.1074/jbc.M000709200 on March 27, 2000

J. Biol. Chem., Vol. 275, Issue 22, 16925-16932, June 2, 2000
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Direct Binding and Activation of STAT Transcription Factors by the Herpesvirus saimiri Protein Tip*

David A. HartleyDagger § and Geoffrey M. CooperDagger

From the Dagger  Department of Biology, Boston University, Boston, Massachusetts 02215

The Tip protein from Herpesvirus saimiri specifically binds to and activates the protein tyrosine kinase, p56lck. It has been demonstrated that the expression of Tip in T cells is capable of inducing the DNA binding of members of the signal transducers and activators of transcription (STAT) family of transcription factors. We have examined the mechanism behind which STATs 1 and 3 are activated by Tip expression. Tip becomes tyrosine phosphorylated by p56lck at two sites in the amino-terminal tail region. One site of phosphorylation lies within a consensus YXPQ binding motif for the SH2 domains of STATs 1 and 3. We demonstrate that tyrosine phosphorylation of Tip at this site is required for the binding of STATs, and the induction of STAT dependent transcription. Furthermore, we demonstrate that, similar to STAT activation by v-Src, the optimum induction of STAT-dependent transcription by Tip requires Ras/Rac mediated signaling events.

* This work was supported in part by National Institutes of Health Grants R01 CA18689 and CA42350.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.

§ Supported by the American Cancer Society post-doctoral fellowship PF-4483. To whom correspondence should be addressed: Dept. of Biology, Boston University, 5 Cummington St., Boston, MA. 02215. Tel.: 617-353-8731; Fax: 617-353-8484.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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