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J Biol Chem, Vol. 274, Issue 7, 3946-3952, February 12, 1999

beta -Subunit of Nuclear Pore-targeting Complex (Importin-beta ) Can Be Exported from the Nucleus in a Ran-independent Manner

Shingo KoseDagger , Naoko ImamotoDagger , Taro TachibanaDagger , Minoru Yoshida§, and Yoshihiro YonedaDagger

From the Dagger  Department of Anatomy and Cell Biology, Osaka University Medical School, 2-2 Yamada-oka, Suita, Osaka 565-0871, Japan and the § Department of Biotechnology, Graduate School of Agriculture and Life Sciences, University of Tokyo, Bunkyo-ku, Tokyo 113-0033, Japan

The nuclear export of importin-alpha is mediated by CAS, which is related to importin-beta , whereas the mechanism for the export of importin-beta remains unclear. In this study, we demonstrate that the nuclear export of importin-beta is mediated by the nuclear pore complex-binding domain of this molecule. Insensitivity to leptomycin B indicates that its export is not mediated by a leucine-rich nuclear export signal-specific receptor, CRM1. Furthermore, the nuclear export of importin-beta was not inhibited by co-injection with a GTPase-deficient Ran mutant (G19V). The cell line tsBN2 contains a temperature-sensitive point mutation in the RCC1 gene, which encodes a guanine nucleotide exchange factor of Ran. At the nonpermissive temperature, importin-beta was exported from the nucleus of these cells, even when RanGAP1, a GTPase-activating protein for Ran, was co-injected. These results not only provide support for the view that Ran-dependent GTP hydrolysis is not required for the nuclear export of importin-beta but also indicate that nuclear RanGTP is not essential for its export. As a result, we propose that importin-beta can be recycled from the nucleus alone in a Ran-independent manner.


Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.



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