肌球蛋白重链磷酸化位点在活细胞胞质分裂过程中调节肌球蛋白定位。
Myosin heavy chain phosphorylation sites regulate myosin localization during cytokinesis in live cells.
作者信息
Sabry J H, Moores S L, Ryan S, Zang J H, Spudich J A
机构信息
Department of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305, USA.
出版信息
Mol Biol Cell. 1997 Dec;8(12):2605-15. doi: 10.1091/mbc.8.12.2605.
Abstract
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.
摘要
传统肌球蛋白II在胞质分裂过程中发挥着重要作用，它以双极粗丝的形式存在，被认为是产生细胞分裂所需力量的分子马达。在盘基网柄菌中，粗丝的形成受肌球蛋白重链尾部区域三个苏氨酸残基磷酸化的调控。我们在此报告这种调控对正在进行胞质分裂的活细胞中肌球蛋白定位的影响。我们对绿色荧光蛋白与野生型肌球蛋白以及三个关键苏氨酸已分别被替换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，粗丝形成是肌球蛋白在分裂沟中积累所必需的，并且如果粗丝过量产生，这种积累会显著增强。这表明分裂细胞中肌球蛋白的定位受肌球蛋白重链磷酸化的调控。
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