Nucleoporins Nup98 and Nup214 Participate in Nuclear Export of Human Immunodeficiency Virus Type 1 Rev

Zolotukhin, Andrei S.; Felber, Barbara K.

doi:10.1128/jvi.73.1.120-127.1999

Cited by 146 publications

(69 citation statements)

References 51 publications

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“…3, row 1). As previously observed [28,30,31], Myc-Rev expression induced CRM1 relocalization and prominent colocalization of Rev and CRM1 in nucleoli ( Fig. 3, row 2).…”

Section: Crm1 Is Critical For the Nullbasic-mediated Redistribution Osupporting

confidence: 87%

Nullbasic, a Potent Anti-HIV Tat Mutant, Induces CRM1-Dependent Disruption of HIV Rev Trafficking

et al. 2012

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Nullbasic, a mutant of the HIV-1 Tat protein, has anti-HIV-1 activity through mechanisms that include inhibition of Rev function and redistribution of the HIV-1 Rev protein from the nucleolus to the nucleoplasm and cytoplasm. Here we investigate the mechanism of this effect for the first time, establishing that redistribution of Rev by Nullbasic is not due to direct interaction between the two proteins. Rather, Nullbasic affects subcellular localization of cellular proteins that regulate Rev trafficking. In particular, Nullbasic induced redistribution of exportin 1 (CRM1), nucleophosmin (B23) and nucleolin (C23) from the nucleolus to the nucleus when Rev was coexpressed, but never in its absence. Inhibition of the Rev:CRM1 interaction by leptomycin B or a non-interacting RevM10 mutant completely blocked redistribution of Rev by Nullbasic. Finally, Nullbasic did not inhibit importin β- or transportin 1-mediated nuclear import, suggesting that cytoplasmic accumulation of Rev was due to increased export by CRM1. Overall, our data support the conclusion that CRM1-dependent subcellular redistribution of Rev from the nucleolus by Nullbasic is not through general perturbation of either nuclear import or export. Rather, Nullbasic appears to interact with and disrupt specific components of a Rev trafficking complex required for its nucleocytoplasmic shuttling and, in particular, its nucleolar accumulation.

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“…3, row 1). As previously observed [28,30,31], Myc-Rev expression induced CRM1 relocalization and prominent colocalization of Rev and CRM1 in nucleoli ( Fig. 3, row 2).…”

Section: Crm1 Is Critical For the Nullbasic-mediated Redistribution Osupporting

confidence: 87%

Nullbasic, a Potent Anti-HIV Tat Mutant, Induces CRM1-Dependent Disruption of HIV Rev Trafficking

et al. 2012

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“…The nucleolus is also emerging as an important target of various viral proteins [4]. Viral proteins targeting the nucleolus are for example implicated in the regulation of apoptosis, as shown with West Nile virus capsid protein, and in the regulation of viral mRNA export, as shown with human immunodeficiency virus Rev protein and with herpesvirus saimiri ORF57 protein [5][6][7]. However, for most viruses, consequences of viral protein localization in the nucleolus remain largely unknown [3,4].…”

Section: Resultsmentioning

confidence: 99%

Nucleolar localization of influenza A NS1: striking differences between mammalian and avian cells

Volmer

Mazel-Sanchez

Volmer

et al. 2010

Virol J

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In mammalian cells, nucleolar localization of influenza A NS1 requires the presence of a C-terminal nucleolar localization signal. This nucleolar localization signal is present only in certain strains of influenza A viruses. Therefore, only certain NS1 accumulate in the nucleolus of mammalian cells. In contrast, we show that all NS1 tested in this study accumulated in the nucleolus of avian cells even in the absence of the above described C-terminal nucleolar localization signal. Thus, nucleolar localization of NS1 in avian cells appears to rely on a different nucleolar localization signal that is more conserved among influenza virus strains.

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“…The accumulation of Rip1p at two distinct NPC sites may reflect rate-limiting steps during that process. The vertebrate NPC-associated FGnucleoporins Nup98 and Nup153 recently have been proposed to move between the nuclear and cytoplasmic compartments in association with exported cargoes (Nakielny et al, 1999;Zolotukhin and Felber, 1999) An association of Rip1p with RNP cargo was suggested by the identification of an interaction between the human RNA export factor TAP and the FG-nucleoporins CAN/ Nup214 and hCG1, the functional homologues of Nup159p and Rip1p, respectively (Katahira et al, 1999;E.Izaurralde, personal communication;and Figure 2). These data support the view that TAP and its yeast homologue Mex67p promote the export of bound RNPs through an interaction with one or more FG-nucleoporins (de Castillia and Rout, 1999).…”

Section: Discussionmentioning

confidence: 98%

The RNA export factor Gle1p is located on the cytoplasmic fibrils of the NPC and physically interacts with the FG-nucleoporin Rip1p, the DEAD-box protein Rat8p/Dbp5p and a new protein Ymr255p

Fahrenkrog²,

et al. 1999

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Y.Strahm and B.Fahrenkrog contributed equally to this workGle1p is an essential, nuclear pore complex (NPC)-associated RNA export factor. In a screen for high copy suppressors of a GLE1 mutant strain, we identified the FG-nucleoporin Rip1p and the DEAD-box protein Rat8p/Dbp5p, both of which have roles in RNA export; we also found Ymr255p/Gfd1p, a novel inessential protein. All three high copy suppressors interact with the C-terminal domain of Gle1p; immunoelectron microscopy localizations indicate that Gle1p, Rip1p and Rat8p/Dbp5p are present on the NPC cytoplasmic fibrils; Rip1p was also found within the nucleoplasm and on the nuclear baskets. In vivo localizations support the hypothesis that Rip1p contributes to the association of Gle1p with the pore and that Gle1p, in turn, provides a binding site for Rat8p/Dbp5p at the NPC. These data are consistent with the view that Gle1p, Rip1p, Rat8p/ Dbp5p and Ymr255p/Gfd1p associate on the cytoplasmic side of the NPC to act in a terminal step of RNA export. We also describe a human functional homologue of Rip1p, called hCG1, which rescues Rip1p function in yeast, consistent with the evolutionary conservation of this NPC-associated protein.

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Nucleoporins Nup98 and Nup214 Participate in Nuclear Export of Human Immunodeficiency Virus Type 1 Rev

Cited by 146 publications

References 51 publications

Nullbasic, a Potent Anti-HIV Tat Mutant, Induces CRM1-Dependent Disruption of HIV Rev Trafficking

Nullbasic, a Potent Anti-HIV Tat Mutant, Induces CRM1-Dependent Disruption of HIV Rev Trafficking

Nucleolar localization of influenza A NS1: striking differences between mammalian and avian cells

The RNA export factor Gle1p is located on the cytoplasmic fibrils of the NPC and physically interacts with the FG-nucleoporin Rip1p, the DEAD-box protein Rat8p/Dbp5p and a new protein Ymr255p

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