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J Biol Chem, Vol. 274, Issue 7, 3946-3952, February 12, 1999
-Subunit of Nuclear Pore-targeting Complex (Importin-
) Can
Be Exported from the Nucleus in a Ran-independent Manner
,
,
,
From the The nuclear export of importin-
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
is mediated by
CAS, which is related to importin-
, whereas the mechanism for the
export of importin-
remains unclear. In this study, we demonstrate
that the nuclear export of importin-
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-
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-
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-
but also indicate that nuclear RanGTP is
not essential for its export. As a result, we propose that importin-
can be recycled from the nucleus alone in a Ran-independent manner.
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