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First published online 19 March 2009
doi: 10.1242/jcs.040154
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Research Article |
1 Department of Biochemistry I, Faculty of Medicine, Georg-August-University of Göttingen, Humboldtallee 23, 37073, Göttingen, Germany
2 Wellcome Trust Centre for Gene Regulation and Expression, MSI/WTB Complex, University of Dundee, Dundee DD1 5EH, UK
3 Heinrich-Pette-Institute for Experimental Virology and Immunology, Martinistrasse 52, 20251 Hamburg, Germany
* Author for correspondence (e-mail: rkehlen{at}gwdg.de)
Accepted 3 December 2008
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 transportin-dependent proteins was also significantly reduced in Nup358-depleted cells. Our data therefore suggest a general role for Nup358 in transportin-mediated nuclear import.
Key words: Nup358, Transportin, Nuclear import, HIV-1 Rev, Nuclear pore complex
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