HIV-1 Vpr interacts with the nuclear transport pathway to promote macrophage infection.

@article{citeulike:3134251, abstract = {HIV-1 Vpr promotes nuclear entry of viral nucleic acids in nondividing macrophages and also causes a G2 cell-cycle arrest. Consistent with its role in nuclear transport, we show Vpr localizes to the nuclear envelope in both human and yeast cells. Like the importin-beta subunit of the nuclear import receptor, Vpr also interacts with the yeast importin-alpha subunit and nucleoporins. Moreover, overexpression of either Vpr or importin-beta in yeast blocks nuclear transport of mRNAs. A mutant form of Vpr (Vpr F34I) that does not localize at the nuclear envelope, or bind to importin-alpha and nucleoporins, renders HIV-1 incapable of infecting macrophages efficiently. Vpr F34I, however, still causes a G2 arrest, demonstrating that the dual functions of Vpr are genetically separable. Our data suggest Vpr functionally resembles importin-beta in nuclear import of the HIV-1 pre-integration complex and this function is essential for the role of Vpr in macrophage infection, but not G2 arrest.}, address = {Divisions of Molecular Medicine and Basic Science, Fred Hutchinson Cancer Research Center, Seattle, Washington 98109 USA.}, author = {Vodicka, M. A. and Koepp, D. M. and Silver, P. A. and Emerman, M. }, citeulike-article-id = {3134251}, issn = {0890-9369}, journal = {Genes \& development}, keywords = {hiv, vpr}, month = {January}, number = {2}, pages = {175--185}, posted-at = {2008-08-18 21:47:14}, priority = {2}, title = {HIV-1 Vpr interacts with the nuclear transport pathway to promote macrophage infection.}, url = {http://view.ncbi.nlm.nih.gov/pubmed/9436978}, volume = {12}, year = {1998} }

TY - JOUR ID - citeulike:3134251 L3 - citeulike-article-id:3134251 N2 - HIV-1 Vpr promotes nuclear entry of viral nucleic acids in nondividing macrophages and also causes a G2 cell-cycle arrest. Consistent with its role in nuclear transport, we show Vpr localizes to the nuclear envelope in both human and yeast cells. Like the importin-beta subunit of the nuclear import receptor, Vpr also interacts with the yeast importin-alpha subunit and nucleoporins. Moreover, overexpression of either Vpr or importin-beta in yeast blocks nuclear transport of mRNAs. A mutant form of Vpr (Vpr F34I) that does not localize at the nuclear envelope, or bind to importin-alpha and nucleoporins, renders HIV-1 incapable of infecting macrophages efficiently. Vpr F34I, however, still causes a G2 arrest, demonstrating that the dual functions of Vpr are genetically separable. Our data suggest Vpr functionally resembles importin-beta in nuclear import of the HIV-1 pre-integration complex and this function is essential for the role of Vpr in macrophage infection, but not G2 arrest. IS - 2 JF - Genes & development SN - 0890-9369 AD - Divisions of Molecular Medicine and Basic Science, Fred Hutchinson Cancer Research Center, Seattle, Washington 98109 USA. EP - 185 TI - HIV-1 Vpr interacts with the nuclear transport pathway to promote macrophage infection. VL - 12 SP - 175 KW - hiv KW - vpr AU - Vodicka, MA AU - Koepp, DM AU - Silver, PA AU - Emerman, M PY - 1998/01/15/ UR - http://view.ncbi.nlm.nih.gov/pubmed/9436978 ER -