The nuclear pore component Nup358 promotes transportin-dependent nuclear import

Abstract

Nup358 (also known as RanBP2), a component of the cytoplasmic filaments of the nuclear pore complex, has been implicated in various nucleocytoplasmic transport pathways. Here, we identify Nup358 as an important factor for transportin-mediated nuclear import. Depletion of Nup358 resulted in a strong inhibition of nuclear import of the human immunodeficiency virus type 1 (HIV-1) Rev protein. HIV-1 Rev is an RNA-binding protein that is required for CRM1 (also known as exportin 1)-dependent nuclear export of unspliced or partially spliced viral RNA. We show that transportin is the major nuclear import receptor for HIV-1 Rev in HeLa cells. Overexpression of transportin strongly promoted nuclear import of HIV-1 Rev in Nup358-depleted cells, indicating that the import receptor becomes rate-limiting under these conditions. Importantly, the import rate of other transportindependent proteins was also significantly reduced in Nup358-depleted cells. Our data therefore suggest a general role for Nup358 in transportin-mediated nuclear import. Supplementary material available online at

The Anti-inflammatory Prostaglandin 15-Deoxy-Δ12,14-PGJ2 Inhibits CRM1-dependent Nuclear Protein Export

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Cellular and viral determinants of retroviral nuclear entry

“…However, in a cell-based co-immunoprecipitation assay, a significant reduction in HIV-1 production was noted in importin 7 knockout cells, indicating that the IN bipartite NLS interacts with importin 7 and not importin 8 in vivo (Ao et al 2007). Another NLS-containing HIV-1 protein, Rev, is rich in the basic amino acid arginine (instead of lysine) and prefers to interact with transportin and importins 5, 7, and 9 in vitro independent of importin ␣ (Arnold et al 2006;Hutten et al 2009). This preference may be dependent on the concentration of each import receptor or competition between import cargo.…”

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