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MBC in Press, published online ahead of print April 23, 2008
Mol. Biol. Cell 10.1091/mbc.E08-02-0198

A more recent version of this article appeared on July 1, 2008
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Submitted on February 25, 2008
Revised on March 31, 2008
Accepted on April 10, 2008

Aurora a Phosphorylates MCAK to Control Ran-dependent Spindle Bipolarity

Xin Zhang, Stephanie C. Ems-McClung, and Claire E. Walczak

Department of Biochemistry and Molecular Biology and Department of Medical Sciences, Indiana University, Bloomington, IN 47405

Monitoring Editor: Stephen Doxsey

During mitosis MCAK localizes to chromatin/kinetochores, a cytoplasmic pool, and spindle poles. Its localization and activity in the chromatin region are regulated by Aurora B kinase; however, how the cytoplasmic and pole localized MCAK are regulated is currently not clear. In this study we used Xenopus egg extracts to form spindles in the absence of chromatin and centrosomes and found that MCAK localization and activity are tightly regulated by Aurora A. This regulation is important to focus microtubules at aster centers and to facilitate the transition from asters to bipolar spindles. In particular, we found that MCAK colocalized with NuMA and XMAP215 at the center of Ran asters where its activity is regulated by Aurora A-dependent phosphorylation of S196, which contributes to proper pole focusing. In addition we found that MCAK localization at spindle poles was regulated through another Aurora A phosphorylation site (S719), which positively enhances bipolar spindle formation. This is the first study that clearly defines a role for MCAK at the spindle poles as well as identifies another key Aurora A substrate that contributes to spindle bipolarity.

Address correspondence to: Claire E. Walczak (cwalczak{at}indiana.edu)






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