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Originally published In Press as doi:10.1074/jbc.M200522200 on May 24, 2002

J. Biol. Chem., Vol. 277, Issue 32, 28521-28529, August 9, 2002
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Subunit H of the V-ATPase Binds to the Medium Chain of Adaptor Protein Complex 2 and Connects Nef to the Endocytic Machinery*

Matthias GeyerDagger §, Haifeng Yu§, Robert Mandic, Thomas Linnemann, Yong-Hui Zheng, Oliver T. Fackler||, and B. Matija Peterlin**

From the Departments of Medicine, Microbiology and Immunology, University of California, San Francisco, California 94143-0703, the Dagger  Max-Planck-Institute for Molecular Physiology, Department of Physical Biochemistry, 44227 Dortmund, Germany, the  Department of Otorhinolaryngology, Head and Neck Surgery, University of Marburg, 35037 Marburg, Germany, and the || Institute for Hygiene, Department of Virology, University of Heidelberg, 69120 Heidelberg, Germany

Nef is an accessory protein of human and simian immunodeficiency viruses (HIV and SIV) that is required for efficient viral infectivity and pathogenicity. It decreases the expression of CD4 on the surface of infected cells. V1H is the regulatory subunit H of the vacuolar membrane ATPase (V-ATPase). Previously, the interaction between Nef and V1H has been found to facilitate the internalization of CD4, suggesting that V1H could connect Nef to the endocytic machinery. In this study, we demonstrate that V1H binds to the C-terminal flexible loop in Nef from HIV-1 and to the medium chain (µ2) of the adaptor protein complex 2 (AP-2) in vitro and in vivo. The interaction sites of V1H and µ2 were mapped to a central region in V1H from positions 133 to 363, which contains 4 armadillo repeats, and to the N-terminal adaptin-binding domain in µ2 from positions 1 to 145. Fusing Nef to V1H reproduced the appropriate trafficking of Nef. This chimera internalized CD4 even in the absence of the C-terminal flexible loop in Nef. Finally, blocking the expression of V1H decreased the enhancement of virion infectivity by Nef. Thus, V1H can function as an adaptor for interactions between Nef and AP-2.

* This work was supported in part by grants from the European Molecular Biology Organization, the Peter und Traudl Engelhorn Stiftung (to M. G.), the Deutsche Forschungsgemeinschaft (to T. L. and O. T. F.), the University AIDS Research Program (to Y-H. Z.), the Howard Hughes Medical Institute, and National Institutes of Health Grant 1RO1AI38532-01.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.

§ Both authors contributed equally to this work.

** To whom correspondence should be addressed: University of California, Mt. Zion Cancer Research Center, Rm. 226, Box 0703, 2340 Sutter St., San Francisco, CA 94143-0703. Tel.: 415-502-1902; Fax: 415-502-1901; E-mail: matija@itsa.ucsf.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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