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J. Cell Biol.,
Volume 143, Number 4, November 16, 1998 875-885
* Gladstone Institute of Virology and Immunology, While the Vpr protein of HIV-1 has been implicated in import of the viral preintegration complex
across the nuclear pore complex (NPC) of nondividing
cellular hosts, the mechanism by which Vpr enters the
nucleus remains unknown. We now demonstrate that
Vpr contains two discrete nuclear targeting signals that
use two different import pathways, both of which are
distinct from the classical nuclear localization signal
(NLS)- and the M9-dependent pathways. Vpr import
does not appear to require Ran-mediated GTP hydrolysis and persists under conditions of low energy. Competition experiments further suggest that Vpr directly
engages the NPC at two discrete sites. These sites appear to form distal components of a common import
pathway used by NLS- and M9-containing proteins. Together, our data suggest that Vpr bypasses many of the
soluble receptors involved in import of cellular cargoes.
Rather, this viral protein appears to directly access the
NPC, a property that may help to ensure the capacity of
HIV to replicate in nondividing cellular hosts.
Department of Biochemistry and Biophysics, § Department of Medicine, and Department of Microbiology and Immunology, University of California, San Francisco, California 94141-9100
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