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Vol. 16, Issue 1, 193-201, January 2005
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* Department of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305;
Department of Systems Biology, Harvard Medical School, Boston, MA 02115
Submitted August 31, 2004;
Revised October 6, 2004;
Accepted October 8, 2004
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.
The online version of this article contains supplemental material at MBC Online (http://www.molbiolcell.org).
Corresponding author. E-mail address: astraight{at}stanford.edu.
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