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Originally published In Press as doi:10.1074/jbc.M010533200 on February 16, 2001

J. Biol. Chem., Vol. 276, Issue 19, 15920-15928, May 11, 2001
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The Human Immunodeficiency Virus Type 1 Vpu Protein Inhibits NF-kappa B Activation by Interfering with beta TrCP-mediated Degradation of Ikappa B*

Stephan BourDagger , Christèle PerrinDagger , Hirofumi Akari, and Klaus Strebel§

From the Laboratory of Molecular Microbiology, NIAID, National Institutes of Health, Bethesda, Maryland 20892-0460

The human immunodeficiency virus type 1 (HIV-1) Vpu protein binds to the CD4 receptor and induces its degradation by cytosolic proteasomes. This process involves the recruitment of human beta TrCP (TrCP), a key member of the SkpI-Cdc53-F-box E3 ubiquitin ligase complex that specifically interacts with phosphorylated Vpu molecules. Interestingly, Vpu itself, unlike other TrCP-interacting proteins, is not targeted for degradation by proteasomes. We now report that, by virtue of its affinity for TrCP and resistance to degradation, Vpu, but not a phosphorylation mutant unable to interact with TrCP, has a dominant negative effect on TrCP function. As a consequence, expression of Vpu in HIV-infected T cells or in HeLa cells inhibited TNF-alpha -induced degradation of Ikappa B-alpha . Vpu did not inhibit TNF-alpha -mediated activation of the Ikappa B kinase but instead interfered with the subsequent TrCP-dependent degradation of phosphorylated Ikappa B-alpha . This resulted in a pronounced reduction of NF-kappa B activity. We also observed that in cells producing Vpu-defective virus, NF-kappa B activity was significantly increased even in the absence of cytokine stimulation. However, in the presence of Vpu, this HIV-mediated NF-kappa B activation was markedly reduced. These results suggest that Vpu modulates both virus- and cytokine-induced activation of NF-kappa B in HIV-1-infected cells.

* This work was supported in part by a grant from the Intramural AIDS Targeted Antiviral Program (to K. S.).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 These authors contributed equally to this work.

§ To whom correspondence should be addressed: NIH/NIAID, 4/312, 4 Center Dr., MSC 0460, Bethesda, MD 20892-0460. Tel.: 301-496-3132; Fax: 301-402-0226; E-mail: kstrebel@nih.gov.

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