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Proc Natl Acad Sci U S A ; 102(5): 1478-83, 2005 Feb 01.
Artigo em Inglês | MEDLINE | ID: mdl-15659549

RESUMO

HIV type 1 (HIV-1) was shown to assemble either at the plasma membrane or in the membrane of late endosomes. Now, we report an essential role for human ubiquitin ligase POSH (Plenty of SH3s; hPOSH), a trans-Golgi network-associated protein, in the targeting of HIV-1 to the plasma membrane. Small inhibitory RNA-mediated silencing of hPOSH ablates virus secretion and Gag plasma membrane localization. Reintroduction of native, but not a RING finger mutant, hPOSH restores virus release and Gag plasma membrane localization in hPOSH-depleted cells. Furthermore, expression of the RING finger mutant hPOSH inhibits virus release and induces accumulation of intracellular Gag in normal cells. Together, our results identify a previously undescribed step in HIV biogenesis and suggest a direct function for hPOSH-mediated ubiquitination in protein sorting at the trans-Golgi network. Consequently, hPOSH may be a useful host target for therapeutic intervention.


Assuntos
HIV-1/fisiologia , Ubiquitina-Proteína Ligases/metabolismo , Replicação Viral/fisiologia , Rede trans-Golgi/enzimologia , Membrana Celular/enzimologia , Membrana Celular/virologia , Clonagem Molecular , Produtos do Gene gag/metabolismo , Inativação Gênica , Células HeLa , Humanos , Transporte Proteico , Proteínas Recombinantes/metabolismo , Ubiquitina-Proteína Ligases/genética
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