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(Received for publication, August 13, 1996, and in revised form, October 15, 1996)
From the Department of Anatomy and Cell Biology and the
§ Division of Molecular Oncology, Biomedical Research
Center, Osaka University Medical School, 2-2 Yamada-oka, Suita,
Osaka 565, Japan
In response to interferon-
Volume 271, Number 49,
Issue of December 6, 1996
pp. 31017-31020
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
COMMUNICATION:
-dependent Nuclear Import of Stat1 Is
Mediated by the GTPase Activity of Ran/TC4
(IFN-), Stat1
enters the nucleus, where it activates transcription. In order to
better understand the mechanism of the extracellular signal-induced
protein import into the nucleus, we have established an in
vivo assay system that uses recombinant Stat1 protein as a model
transport substrate. Using this system, we found that Stat1 is actively
transported through the nuclear pores in an
IFN--dependent manner and tyrosine (Tyr701)
phosphorylation of Stat1 is actually required for its nuclear import.
When the antibody against Ran, which was identified as an essential
factor for active nuclear protein transport, was injected, the
IFN--dependent nuclear transport of Stat1 was completely inhibited. Furthermore, nuclear import of Stat1 was suppressed by
microinjection of two mutant Ran proteins, one defective in GTP
hydrolysis (G19V) and the other with little or no binding to GTP
(T24N), both of which are known to act as dominant negative inhibitors
of nuclear import. These results indicate that the conditional nuclear
import of Stat1 requires GTP hydrolysis by Ran.
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