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Papers In Press, published online ahead of print April 3, 2002
Center for Cell Signaling, University of Virginia, Charlottesville, VA 22908
Corresponding Author: amb7c{at}virginia.edu
Ran-binding protein 3 (RanBP3)1 is an ~55-kD protein that functions as a cofactor for Crm1-mediated nuclear export. RanBP3 stimulates export by enhancing the affinity of Crm1 for Ran:GTP and cargo. However, there may exist important additional functions for this cofactor. We now report that RanBP3 associates with the Ran-specific guanine nucleotide exchange factor RCC1. This interaction was stimulated by the addition of Ran; moreover, Ran:GDP, Ran:GTP, and Ran without nucleotide could all stimulate complex formation between RanBP3 and RCC1, even though binding of Ran:GDP to RanBP3 alone was undetectable. RanBP3 could also promote binding of Crm1 to RCC1 in the presence of Ran. Binding of RanBP3 to RCC1 increased the catalytic activity of RCC1 towards Ran and, importantly, the ability of RanBP3 to stimulate RCC1 was not affected by the presence of Crm1. These data indicate that RanBP3 acts as a scaffold protein to promote the efficient assembly of export complexes. By tethering Crm1 to catalytically enhanced RCC1, RanBP3 may lower the entropic barrier for the loading of Ran:GTP onto Crm1. We propose that this provides an additional mechanism by which RanBP3 facilitates export.
J. Biol. Chem, 10.1074/jbc.C100620200
Submitted on October 26, 2001
Revised on March 27, 2002
Accepted on April 2, 2002
Ran-binding protein 3 links Crm1 to the Ran exchange factor RCC1
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