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Vol. 12, Issue 3, 539-549, March 2001

The Nuclear Export Receptor Xpo1p Forms Distinct Complexes with NES Transport Substrates and the Yeast Ran Binding Protein 1 (Yrb1p)

Patrick Maurer,^* Michael Redd,^@ Jens Solsbacher,^* F. Ralf Bischoff, Markus Greiner,^* Alexandre V. Podtelejnikov,^§ Matthias Mann,^§ Katrin Stade, Karsten Weis, and Gabriel Schlenstedt^*

 ^*Medizinische Biochemie und Molekularbiologie, Universität des Saarlandes, 66421 Homburg, Germany;  Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720, USA;  Molekulare Biologie der Mitose, Deutsches Krebsforschungszentrum, 69120 Heidelberg, Germany;  ^§Protein Interaction Laboratory, University of Southern Denmark, 5230 Odense, Denmark;  Max-Delbrück-Centrum für Molekulare Medizin, Robert-Rössle-Str. 10, 13029 Berlin, Germany.

Xpo1p (Crm1p) is the nuclear export receptor for proteins containing a leucine-rich nuclear export signal (NES). Xpo1p, the NES-containing protein, and GTP-bound Ran form a complex in the nucleus that translocates across the nuclear pore. We have identified Yrb1p as the major Xpo1p-binding protein in Saccharomyces cerevisiae extracts in the presence of GTP-bound Gsp1p (yeast Ran). Yrb1p is cytoplasmic at steady-state but shuttles continuously between the cytoplasm and the nucleus. Nuclear import of Yrb1p is mediated by two separate nuclear targeting signals. Export from the nucleus requires Xpo1p, but Yrb1p does not contain a leucine-rich NES. Instead, the interaction of Yrb1p with Xpo1p is mediated by Gsp1p-GTP. This novel type of export complex requires the acidic C-terminus of Gsp1p, which is dispensable for the binding to importin -like transport receptors. A similar complex with Xpo1p and Gsp1p-GTP can be formed by Yrb2p, a relative of Yrb1p predominantly located in the nucleus. Yrb1p also functions as a disassembly factor for NES/Xpo1p/Gsp1p-GTP complexes by displacing the NES protein from Xpo1p/Gsp1p. This Yrb1p/Xpo1p/Gsp1p complex is then completely dissociated after GTP hydrolysis catalyzed by the cytoplasmic GTPase activating protein Rna1p.

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Present addresses: ^@Department of Anatomy and Developmental Biology, University College London, Gower Street, London, WC1E 6BT, United Kingdom; Aventis Research and Technologies GmbH, Operative Forschung, 65926 Frankfurt, Germany.

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Molecular Biology of the Cell
Vol. 12, 539-549, March 2001
Copyright © 2001 by The American Society for Cell Biology

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