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新型肌球蛋白。

Novel myosins.

作者信息

Hammer J A

机构信息

Laboratory of Cell Biology, Bldg 3, Rm B1-22, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892, USA.

出版信息

Trends Cell Biol. 1991 Aug;1(2-3):50-6. doi: 10.1016/0962-8924(91)90089-r.

Abstract

The traditional view of myosin, drawn from studies of myosins from striated muscles, is that of an elongated two-headed molecule that assembles into filaments. However, biochemical, molecular genetic and genetic studies have uncovered a host of ubiquitous single-headed nonfilamentous myosins known collectively as myosins I. All of the myosins I possess the myosin head domain, the motor portion of muscle myosins they have tail the filament-forming tail domain of muscle myosins they have tail domains that interact variously with membranes, actin and calmodulin. These alternative molecular interactions confer novel motile properties on myosins I, such as the ability to move membranes relative to actin and to move actin relative to actin without having to assemble into filaments. The numerous actin-based movements retained by cells lacking myosin II, the two-headed filamentous form of nonmuscle myosin, may be supported by myosins I.

摘要

基于对横纹肌肌球蛋白的研究,传统上对肌球蛋白的看法是,它是一种细长的双头分子,能组装成细丝。然而,生物化学、分子遗传学和遗传学研究发现了许多普遍存在的单头无丝状肌球蛋白,统称为肌球蛋白I。所有的肌球蛋白I都拥有肌球蛋白头部结构域,即肌肉肌球蛋白的运动部分,它们有尾巴,有肌肉肌球蛋白的丝状尾巴结构域,还有能与膜、肌动蛋白和钙调蛋白发生不同相互作用的尾巴结构域。这些不同的分子相互作用赋予了肌球蛋白I新的运动特性,比如使膜相对于肌动蛋白移动以及使肌动蛋白相对于肌动蛋白移动的能力,而无需组装成细丝。缺乏肌球蛋白II(非肌肉肌球蛋白的双头丝状形式)的细胞所保留的众多基于肌动蛋白的运动,可能由肌球蛋白I来支持。

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