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Originally published In Press as doi:10.1074/jbc.M011087200 on January 30, 2001

J. Biol. Chem., Vol. 276, Issue 17, 14524-14531, April 27, 2001
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Stimulation of Nuclear Export and Inhibition of Nuclear Import by a Ran Mutant Deficient in Binding to Ran-binding Protein 1*

Ralph H. KehlenbachDagger §, Ralf Assheuer, Angelika KehlenbachDagger , Jörg Becker, and Larry GeraceDagger

From the Dagger  Departments of Cell and Molecular Biology, The Scripps Research Institute, La Jolla, California 92037 and the  Max-Planck-Institut für Molekulare Physiologie, 11 Otto-Hahn-Strasse, Dortmund 44227, Germany

Receptor-mediated nucleocytoplasmic transport is dependent on the GTPase Ran and Ran-binding protein 1 (RanBP1). The acidic C terminus of Ran is required for high affinity interaction between Ran and RanBP1. We found that a novel Ran mutant with four of its five acidic C-terminal amino acids modified to alanine (RanC4A) has an ~20-fold reduced affinity for RanBP1. We investigated the effects of RanC4A on nuclear import and export in permeabilized HeLa cells. Although RanC4A promotes accumulation of the nuclear export receptor CRM1 at the cytoplasmic nucleoporin Nup214, it strongly stimulates nuclear export of GFP-NFAT. Since RanC4A exhibits an elevated affinity for CRM1 and other nuclear transport receptors, this suggests that formation of the export complex containing CRM1, Ran-GTP, and substrate is a rate-limiting step in export, not release from Nup214. Conversely, importin alpha /beta -dependent nuclear import of bovine serum albumin, coupled to a classical nuclear localization sequence is strongly inhibited by RanC4A. Inhibition can be reversed by additional importin alpha , which promotes the formation of an importin alpha /beta complex. These results provide physiological evidence that release of Ran-GTP from importin beta  by RanBP1 and importin alpha  is critical for the recycling of importin beta  to a transport-competent state.

* This work was supported by National Institutes of Health Grant GM41955 (to L. G.) and Deutsche Forschungsgemeinschaft Grant 1432 2-1 (to J. B.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ To whom correspondence should be addressed: Universität Heidelberg, Abteilung Virologie, Im Neuenheimer Feld 324, 69120 Heidelberg, Germany. Tel.: 49 6221 561325; Fax: 49 6221 565003; E-mail: Ralph.Kehlenbach@med.uni-heidelberg.de.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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