Regulation and recycling of myosin V.
Regulation and recycling of myosin V.
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DOI：
10.1016/j.ceb.2006.12.014
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发表时间：
2007-02
影响因子：
7.5
通讯作者：
K. Taylor
中科院分区：
文献类型：
--
作者：
K. Taylor
近年来，通过阐明非传统肌球蛋白V非活性构象的结构和影响该构象稳定性的因素，我们对非常规肌球蛋白V的调控有了很大的了解。非活性构象是一种折叠紧凑的结构，其特征是肌球蛋白头部和C末端货物结合域之间的相互作用。当Ca~(2+)浓度大于10μM时，会破坏折叠。在一项研究中通过二维阵列的冷冻电子断层扫描确定的三维结构，以及在另一项研究中报告的分离分子的电子显微镜照片显示了类似的特征，但表明不同的F-肌动蛋白亲和力对于不活跃的构象。这就提出了一个问题，即不活跃的肌球蛋白V是如何被回收到其他地点进行额外的货物运输的。
Recently there has been considerable progress in our understanding of regulation for unconventional myosin-V through elucidation of the structure of its inactive conformation and the factors that affect stability of this conformation. The inactive conformation is a folded compact structure characterized by interactions between the myosin head and the C-terminal cargo binding domain. Concentrations of Ca2+greater than 10μM disrupt folding. The 3-D structure determined by cryoelectron tomography of 2-D arrays in one study and electron micrographs of isolated molecules reported in another reveal similar features, but suggest different F-actin affinities for the inactive conformation. This has raised the question of how inactive myosin-V is recycled to other sites for additional rounds of cargo transport.