Myosin heavy chain phosphorylation sites regulate myosin localization during cytokinesis in live cells
Myosin heavy chain phosphorylation sites regulate myosin localization during cytokinesis in live cells
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DOI：
10.1091/mbc.8.12.2605
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发表时间：
1997-12-01
影响因子：
3.3
通讯作者：
Spudich, JA
中科院分区：
文献类型：
--
作者：
Sabry, JH;Moores, SL;Spudich, JA
常规肌球蛋白II在细胞分裂过程中起着重要作用，以双极粗丝的形式，被认为是产生分裂细胞所需力量的分子马达。在盘基骨桥菌中，粗丝的形成受肌球蛋白重链尾部三个苏氨酸残基的磷酸化调控。我们在这里报告了这种调节对肌球蛋白在细胞分裂活细胞中的定位的影响。我们对绿色荧光蛋白与野生型肌球蛋白和与三个关键苏氨酸被改变为丙氨酸或天冬氨酸的肌球蛋白的融合蛋白进行了成像。我们提供的证据表明，在卵裂沟中肌球蛋白的积累需要粗丝的形成，如果粗丝过量产生，这种积累明显增强。这表明肌凝蛋白在分裂细胞中的定位受肌凝蛋白重链磷酸化的调控。
Conventional myosin II plays a fundamental role in the process of cytokinesis where, in the form of bipolar thick filaments, it is thought to be the molecular motor that generates the force necessary to divide the cell. In Dictyostelium, the formation of thick filaments is regulated by the phosphorylation of three threonine residues in the tail region of the myosin heavy chain. We report here on the effects of this regulation on the localization of myosin in live cells undergoing cytokinesis. We imaged fusion proteins of the green-fluorescent protein with wild-type myosin and with myosins where the three critical threonines had been changed to either alanine or aspartic acid. We provide evidence that thick filament formation is required for the accumulation of myosin in the cleavage furrow and that if thick filaments are overproduced, this accumulation is markedly enhanced. This suggests that myosin localization in dividing cells is regulated by myosin heavy chain phosphorylation.