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Originally published In Press as doi:10.1074/jbc.M006454200 on April 24, 2001

J. Biol. Chem., Vol. 276, Issue 28, 25804-25812, July 13, 2001
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Protein Phosphatase 2A Activates the HIV-2 Promoter through Enhancer Elements That Include the pets Site*

Neil E. FaulknerDagger , John M. Hilfinger||, and David M. MarkovitzDagger **

From the  Department of Internal Medicine, Division of Infectious Diseases and the Dagger  Cellular & Molecular Biology Program, University of Michigan Medical Center, Ann Arbor, Michigan 48109-0640 and || Therapeutic Systems Research Laboratories, Ann Arbor, Michigan 48108

Human immunodeficiency virus type 2 (HIV-2) gene expression is regulated by upstream promoter elements, including the peri-Ets (pets) site, which mediate enhancer stimulation following treatment with the phorbol ester 12-O-tetradecanoylphorbol-13-acetate (TPA). We previously showed that the oncoprotein DEK binds to the pets site in a site-specific manner. In this report, we show that binding to the HIV-2 pets site is modulated by treatment of U937 monocytic cells with TPA, an activator of protein kinase C. TPA treatment resulted in a reduction in the levels of DEK and the formation of a faster migrating pets complex in gel shift assays. We show further that the actions of TPA on pets binding can be duplicated by phosphatase treatment of nuclear proteins and is blocked with okadaic acid, a protein phospatase-2A (PP2A) inhibitor. Finally, we demonstrate that ectopic expression of the catalytic domain of PP2A can activate the HIV-2 enhancer/promoter alone or in synergy with TPA, an effect mediated in part through the pets site. These results suggest that, through an interaction with the protein kinase C pathway, PP2A is strongly involved in regulating HIV-2 enhancer-mediated transcription. This is a consequence of its effects on DEK expression and binding to the pets site, as well as its effects on other promoter elements. These findings have implications not only for HIV-2 transcription but also for multiple cellular processes involving DEK or PP2A.

* This work was supported by Grant 36685 from NIAID, National Institutes of Health (to D. M. M.) and an American Cancer Society grant.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 a Rackham merit fellowship from the University of Michigan.

** To whom correspondence should be addressed: Dept. of Internal Medicine, Division of Infectious Diseases, 5220 MSRB3, 1150 W. Medical Center Dr., Ann Arbor, MI 48109-0640. Tel.: 734-936-3844; Fax: 734-764-0101; E-mail: dmarkov@umich.edu.

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