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Vol. 15, Issue 1, 46-57, January 2004
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/
and Ran-GTP Regulate XCTK2 Microtubule Binding through a Bipartite Nuclear Localization Signal
* Medical Sciences Program, Indiana University, Bloomington, Indiana 47405;
Department of Embryology, Howard Hughes Medical Institute, Carnegie Institute of Washington, Baltimore, Maryland 21211
Submitted July 1, 2003;
Revised August 13, 2003;
Accepted August 26, 2003
Monitoring Editor: Ted Salmon
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, because 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.
Corresponding author. E-mail address: cwalczak{at}indiana.edu.
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