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J. Biol. Chem., Vol. 280, Issue 39, 33516-33524, September 30, 2005

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Anillin Is a Substrate of Anaphase-promoting Complex/Cyclosome (APC/C) That Controls Spatial Contractility of Myosin during Late Cytokinesis^*

From the Department of Biological Sciences, Stanford University, Stanford, California 94305-5020

Anillin, an actin-binding protein localized at the cleavage furrow, is required for cytokinesis. Through an in vitro expression screen, we identified anillin as a substrate of the anaphase-promoting complex/cyclosome (APC/C), a ubiquitin ligase that controls mitotic progression. We found that the levels of anillin fluctuate in the cell cycle, peaking in mitosis and dropping drastically during mitotic exit. Ubiquitination of anillin required a destruction-box and was mediated by Cdh1, an activator of APC/C. Overexpression of Cdh1 reduced the levels of anillin, whereas inactivation of APC/C^Cdh1 increased the half-life of anillin. Functionally, anillin was required for the completion of cytokinesis. In anillin knockdown cells, the cleavage furrow ingressed but failed to complete the ingression. At late cytokinesis, the cytosol and DNA in knockdown cells underwent rapid myosin-based oscillatory movement across the furrow. During this movement, RhoA and active myosin were absent from the cleavage furrow, and myosin was redistributed to cortical patches, which powers the random oscillatory movement. We concluded that anillin functions to maintain the localization of active myosin, thereby ensuring the spatial control of concerted contraction during cytokinesis.

Received for publication, April 28, 2005 , and in revised form, July 14, 2005.

^* This work was supported in part by grants from National Institutes of Health (Grant GM062852) and from American Cancer Society (Grant RSG-01-143-01-CCG) (to G. F.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains supplemental movies.

¹ Supported by a postdoctoral fellowship from American Heart Association.

² To whom correspondence should be addressed: Dept. of Biological Sciences, Stanford University, 337 Campus Dr., MC-5020, Lokey Chemical Biology Bldg., Rm. 137, Stanford, CA 94305-5020.

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