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J. Biol. Chem., Vol. 279, Issue 42, 43530-43539, October 15, 2004

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The Karyopherin Msn5/Kap142 Requires Nup82 for Nuclear Export and Performs a Function Distinct from Translocation in RPA Protein Import^*

Kenneth D. Belanger, Laura A. Simmons¶, Jessica K. Roth||, Kristin A. VanderPloeg**, Lauren B. Lichten, and Birthe Fahrenkrog

From the Department of Biology, Colgate University, Hamilton, New York 13346 and the Maurice E. Muller Institute for Structural Biology, Biozentrum, University of Basel, CH-4056, Basel, Switzerland

Protein transport between the nucleus and cytoplasm requires interactions between nuclear pore complex proteins (nucleoporins) and soluble nuclear transport factors (karyopherins, importins, and exportins). Exactly how these interactions contribute to the nucleocytoplasmic transport of substrates remains unclear. Using a synthetic lethal screen with the nucleoporin NUP1, we have identified a conditional allele of NUP82, encoding an essential nuclear pore complex protein in Saccharomyces cerevisiae. This nup82-3 allele also exhibits synthetic genetic interactions with mutants of the karyopherin MSN5. nup82-3 mutants accumulate the Msn5 export substrate Pho4 within the nucleus at non-permissive temperatures. The nuclear import of the RPA complex subunit Rfa2 is impaired in nup82-3 and in mutants of the karyopherin KAP95, but is not affected by the loss of MSN5. Interestingly, deletion of MSN5 results in retention of Rfa2-GFP within the nucleus under conditions in which it normally diffuses out. These data provide evidence that Nup82 is important for Msn5-mediated nuclear protein export and Kap95-mediated protein import. In addition, Msn5 may play a role independent of import in the localization of Rfa2.

Received for publication, July 7, 2004

^* This work was supported in part by National Institutes of Health Grant GM-65107 and National Science Foundation Grant DBI-0216408 (to K. D. B.) and the Swiss National Science Foundation (to B. F.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

^¶ Supported by National Institutes of Health summer undergraduate research support Grant GM-65107. Present address: Dept. of Biology, Duke University, Durham, NC 27708.

^|| Present address: Dept. of Microbiology, University of Pennsylvania, Philadelphia, PA 19104.

^** Present address: Washington University School of Medicine, St. Louis, MO 63130.

Supported by a Wolk Summer Undergraduate Research Fellowship from Colgate University. Present address: Genetic Counseling Program, Brandeis University, Waltham, MA 02453.

To whom correspondence should be addressed: Dept. of Biology, Colgate University, 13 Oak Dr., Hamilton, NY 13346. Tel.: 315-228-7870; Fax: 315-228-7997; E-mail: kbelanger{at}mail.colgate.edu.

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