期刊
MOLECULAR BIOLOGY OF THE CELL
卷 16, 期 1, 页码 193-201出版社
AMER SOC CELL BIOLOGY
DOI: 10.1091/mbc.E04-08-0758
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- NIGMS NIH HHS [GM-023928, R01 GM023928] Funding Source: Medline
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM023928] Funding Source: NIH RePORTER
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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