Anillin Binds Nonmuscle Myosin II and Regulates the Contractile Ring

Author:

Straight Aaron F.1,Field Christine M.2,Mitchison Timothy J.2

Affiliation:

1. Department of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305

2. Department of Systems Biology, Harvard Medical School, Boston, MA 02115

Abstract

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.

Publisher

American Society for Cell Biology (ASCB)

Subject

Cell Biology,Molecular Biology

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