Anillin binds nonmuscle myosin II and regulates the contractile ring
Anillin binds nonmuscle myosin II and regulates the contractile ring
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DOI：
10.1091/mbc.e04-08-0758
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发表时间：
2005-01-01
影响因子：
3.3
通讯作者：
Mitchison, TJ
中科院分区：
文献类型：
--
作者：
Straight, AF;Field, CM;Mitchison, TJ
我们证明，收缩环蛋白苯胺直接与非肌肉肌球蛋白II相互作用，这种相互作用是由肌球蛋白轻链磷酸化调节。我们发现，尽管他们的相互作用，苯胺和肌球蛋白II是独立的针对收缩环。在果蝇或人类培养的细胞中，苯胺醛的耗尽导致胞质分裂失败。在胞质分裂后期，缺乏苯胺醛的人类细胞不能通过肌球蛋白II适当调节收缩，并且不能进行释放。我们提出了一个作用，苯胺在空间调节肌球蛋白II的收缩活动在胞质分裂。
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.