Anillin binds nonmuscle myosin II and regulates the contractile ring

Mol Biol Cell. 2005 Jan;16(1):193-201. doi: 10.1091/mbc.e04-08-0758. Epub 2004 Oct 20.


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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Blotting, Western
  • Cell Line
  • Chromatography
  • Chromatography, Affinity
  • Cloning, Molecular
  • Contractile Proteins / metabolism*
  • Cytokinesis
  • Cytoskeleton / metabolism
  • DNA / metabolism
  • Drosophila
  • HeLa Cells
  • Humans
  • Immunoprecipitation
  • Interphase
  • Metaphase
  • Microscopy, Fluorescence
  • Molecular Sequence Data
  • Muscle Contraction
  • Myosin Type II / metabolism*
  • Myosins / chemistry
  • Phosphorylation
  • Protein Binding
  • RNA / metabolism
  • RNA Interference
  • RNA, Double-Stranded / metabolism
  • Sequence Homology, Amino Acid
  • Xenopus laevis


  • Contractile Proteins
  • RNA, Double-Stranded
  • anillin
  • RNA
  • DNA
  • Myosin Type II
  • Myosins