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J. Biol. Chem., Vol. 277, Issue 32, 28521-28529, August 9, 2002
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From the Departments of Medicine, Microbiology and Immunology,
University of California, San Francisco, California 94143-0703, the
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.
Subunit H of the V-ATPase Binds to the Medium Chain of Adaptor
Protein Complex 2 and Connects Nef to the Endocytic
Machinery*
§,
, and 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
*
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.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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