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- W2146847077 abstract "HIV-1 Vpr promotes nuclear entry of viral nucleic acids in nondividing macrophages and also causes a G 2 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-β subunit of the nuclear import receptor, Vpr also interacts with the yeast importin-α subunit and nucleoporins. Moreover, overexpression of either Vpr or importin-β 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-α and nucleoporins, renders HIV-1 incapable of infecting macrophages efficiently. Vpr F34I, however, still causes a G 2 arrest, demonstrating that the dual functions of Vpr are genetically separable. Our data suggest Vpr functionally resembles importin-β 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 G 2 arrest." @default.
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- W2146847077 date "1998-01-15" @default.
- W2146847077 modified "2023-10-14" @default.
- W2146847077 title "HIV-1 Vpr interacts with the nuclear transport pathway to promote macrophage infection" @default.
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- W2146847077 doi "https://doi.org/10.1101/gad.12.2.175" @default.
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