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Volume 272, Number 1, Issue of January 3, 1997 pp. 551-555
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

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Ran-binding Protein 1 (RanBP1) Forms a Ternary Complex with Ran and Karyopherin  and Reduces Ran GTPase-activating Protein (RanGAP) Inhibition by Karyopherin

(Received for publication, October 22, 1996)

From the Department of Pathology, University of Vermont, and the Vermont Cancer Center, Burlington, Vermont 05405

The nuclear accumulation of proteins containing nuclear localization signals requires the Ran GTPase and a complex of proteins assembled at the nuclear pore. RanBP1 is a cytosolic Ran-binding protein that inhibits RCC1-stimulated release of GTP from Ran. RanBP1 also promotes the binding of Ran to karyopherin  (also called importin  and p97) and is a co-stimulator of RanGAP activity. Yeast karyopherin  inhibits the GTP hydrolysis by Ran catalyzed by RanGAP. To further define the roles of RanBP1 and karyopherin  in Ran function, we explored the effects of RanBP1 and karyopherin  on mammalian proteins known to regulate Ran. Like RanBP1, karyopherin  prevented the release of GTP from Ran stimulated by RCC1 or EDTA. As with the yeast protein, mammalian karyopherin  completely blocked RanGAP activity. However, the addition of RanBP1 to this assay partially rescued the inhibited RanGAP activity. Kinetic analysis of the effects on RanGAP activity by karyopherin  and RanBP1 revealed a combination of competitive and noncompetitive interactions. Solution binding assays confirmed the ability of RanBP1 to associate with Ran and karyopherin  in a ternary complex, and RanBP1 binding was not competed out by the addition of karyopherin . These results demonstrate that RanBP1 and karyopherin  interact with distinct sites of Ran and suggest that RanBP1 plays an essential role in nuclear transport by permitting RanGAP-mediated hydrolysis of GTP on Ran complexed to karyopherin .

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