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Published online 18 June 2001. doi:10.1083/jcb.153.7.1391
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© The Rockefeller University Press, 0021-9525/2001/6/1391/ $5.00
The Journal of Cell Biology, Volume 153, Number 7, June 25, 2001 1391-1402

Original Article

Ran-Binding Protein 3 Is a Cofactor for Crm1-mediated Nuclear Protein Export

Mark E. Lindsaya,b, James M. Holaskaa,b, Katie Welcha,c, Bryce M. Paschala,d, and Ian G. Macaraa,c
a Center for Cell Signaling, University of Virginia School of Medicine, Charlottesville, Virginia 22098
b Departments of Microbiology, University of Virginia School of Medicine, Charlottesville, Virginia 22098
c Department of Pharmacology, University of Virginia School of Medicine, Charlottesville, Virginia 22098
d Department of Biochemistry and Molecular Genetics, University of Virginia School of Medicine, Charlottesville, Virginia 22098

Correspondence to: Mark E. Lindsay, University of Virginia School of Medicine, P.O. Box 800577, Charlottesville, VA 22908-0577. Tel:(804) 982-0083 Fax:(804) 924-1236 E-mail:mel3f{at}virginia.edu.

Crm1 is a member of the karyopherin family of nucleocytoplasmic transport receptors and mediates the export of proteins from the nucleus by forming a ternary complex with cargo and Ran:GTP. This complex translocates through the nuclear pores and dissociates in the cytosol. The yeast protein Yrb2p participates in this pathway and binds Crm1, but its mechanism of action has not been established. We show that the human orthologue of Yrb2p, Ran-binding protein 3 (RanBP3), acts as a cofactor for Crm1-mediated export in a permeabilized cell assay. RanBP3 binds directly to Crm1, and the complex posseses an enhanced affinity for both Ran:GTP and cargo. RanBP3 shuttles between the nucleus and the cytoplasm by a Crm1-dependent mechanism, and the Crm1–RanBP3-NES-Ran:GTP quarternary complex can associate with nucleoporins. We infer that this complex translocates through the nuclear pore to the cytoplasm where it is disassembled by RanBP1 and Ran GTPase–activating protein.

Key Words: Crm1, nuclear export, permeabilized cells, Ran, RanBP3


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