4.4 Article

Anillin binds nonmuscle myosin II and regulates the contractile ring

Journal

MOLECULAR BIOLOGY OF THE CELL
Volume 16, Issue 1, Pages 193-201

Publisher

AMER SOC CELL BIOLOGY
DOI: 10.1091/mbc.E04-08-0758

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Funding

  1. NIGMS NIH HHS [GM-023928, R01 GM023928] Funding Source: Medline
  2. NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM023928] Funding Source: NIH RePORTER

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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.

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