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MBC in Press, published online ahead of print October 20, 2004
Mol. Biol. Cell 10.1091/mbc.E04-08-0758

A more recent version of this article appeared on January 1, 2005
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Submitted on August 31, 2004
Revised on October 6, 2004
Accepted on October 8, 2004

Anillin Binds Nonmuscle Myosin II and Regulates the Contractile Ring

Aaron F. Straight,*{dagger} Christine M. Field,{ddagger} and Timothy J. Mitchison{ddagger}

*Department of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305; {ddagger}Department of Systems Biology, Harvard Medical School, Boston, MA 02115

Monitoring Editor: Yixian Zheng

We demonstrate that the contractile ring protein anillin interacts directly with nonmuscle myosin II and that this interaction is regulated by myosin light chain phosphorylation. We show that despite their interaction, anillin and myosin II are independently targeted to the contractile ring. Depletion of anillin in Drosophila or human cultured cells results in cytokinesis failure. Human cells depleted for anillin fail to properly regulate contraction by myosin II late in cytokinesis and fail in abscission. We propose a role for anillin in spatially regulating the contractile activity of myosin II during cytokinesis.

{dagger}Corresponding author. E-mail: astraight{at}stanford.edu






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