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J. Biol. Chem., Vol. 277, Issue 20, 17385-17388, May 17, 2002
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From the Departments of Ran-binding protein 3 (RanBP3) is an ~55-kDa
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, important additional functions for
this cofactor may exist. We now report that RanBP3 associates with the
Ran-specific guanine nucleotide exchange factor, regulator of
chromosome condensation 1 (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 toward 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.
Microbiology and
§ Pharmacology, The Center for Cell Signaling, The
University of Virginia, Charlottesville, Virginia 22908
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