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A more recent version of this article appeared on January 1, 2004
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Submitted on July 1, 2003
Revised on August 13, 2003
Accepted on August 26, 2003
/
and Ran-GTP regulate XCTK2 microtubule binding through a bipartite NLS
1 Medical Sciences Program, Indiana University, Bloomington, Indiana 47405
2 Howard Hughes Medical Institute, Department of Embryology, Carnegie Institute of Washington, Baltimore, Maryland 21211
* Corresponding author. E-mail address: cwalczak{at}indiana.edu.
The small GTPase Ran is essential for spindle assembly. Ran is
proposed to act through its nuclear import receptors, importin 
and/or importin 
, to control the sequestration of proteins necessary
for spindle assembly. To date, the molecular mechanisms by which the
Ran pathway functions remain unclear. Using purified proteins, we have
reconstituted Ran-regulated microtubule binding of the C-terminal
kinesin XCTK2, a kinesin important for spindle assembly. We show that
the tail of XCTK2 binds to microtubules and that this binding is
inhibited in the presence of importin and (/) and
restored by addition of Ran-GTP. The bipartite nuclear localization
signal (NLS) in the tail of XCTK2 is essential to this process, as
mutation of the NLS abolishes importin /-mediated regulation of
XCTK2 microtubule binding. Our data show that importin / directly
regulates the activity of XCTK2 and that one of the molecular
mechanisms of Ran-regulated spindle assembly is identical to that used
in classical NLS-driven nuclear transport.
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