Mechanism of force production for microtubule-dependent movements.

Mechanism of force production for microtubule-dependent movements.
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DOI:
10.1083/jcb.99.1.132s
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发表时间:
1984-07
期刊:
The Journal of cell biology
影响因子:
--
通讯作者:
Shimizu T
Shimizu T
中科院分区:
其他
文献类型:
--
作者:
Johnson KA;Porter ME;Shimizu T

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我们目前对细胞内颗粒或染色体运动的驱动力的认识主要是基于两种最常见的收缩系统,即基于肌动蛋白-肌球蛋白相互作用或基于微管-动力蛋白相互作用的系统。大量有序排列的材料使得对这些系统中运动机制的研究取得了相当大的进展。有许多例子表明,细胞质肌动蛋白和肌球蛋白参与非肌肉细胞运动(1,2)。支持细胞质动力蛋白参与微管依赖性运动的证据开始积累,最近几个实验室的工作提供了动力蛋白样ATP酶存在于海胆卵有丝分裂纺锤体中的初步证据(3-5)。在解决细胞质动力蛋白样ATP酶的问题时,首先要确定动力蛋白的一般定义,并确定其与肌球蛋白和其他ATP酶区别的特征。动力蛋白被宽泛地定义为与微管相关的ATP酶,具有超过300 kdalton的高分子量多肽(6)。一个更有意义的定义包括它在产生与ATP水解相耦合的运动力方面的直接作用,这必须从系统的生物学和生物化学的角度来探讨。在这篇综述中,我们将总结重要的纤毛动力蛋白的生化特性与肌球蛋白的比较,并与结果的潜在的区别特征的细胞质动力蛋白。
Our current thinking about the driving force for the movements of intracellular particles or chromosomes has been dominated by our knowledge ofthe two most common contractile systems, those based upon actin-myosin interactions or upon microtubule-dynein interactions. Abundant quantities of material in well-ordered arrays have allowed considerable progress to be made in the investigation of the mechanisms responsible for movement in these systems. There are many examples of the involvement of cytoplasmic actin and myosin in nonmuscle cell motility (1, 2). Evidence in favor ofa cytoplasmic dynein in microtubule-dependent motility is beginning to accumulate, and recent work from several laboratories has provided preliminary evidence that a dyneinlike ATPase is present in the mitotic spindle of sea urchin eggs (3-5). In addressing the question of a cytoplasmic dyneinlike ATPase, it is primarily important to establish a general definition ofdynein and to characterize those features that distinguish it from myosin and other ATPases. Dynein has been loosely defined as an ATPase that associates with microtubules and has high molecular weight polypeptides in excess of 300 kdaltons (6). A more meaningful definition includes its direct role in generating a force for movement coupled to the hydrolysis of ATP, which must be approached in terms of the biology as well as the biochemistry of the system. In this review we will summarize the important biochemical properties of ciliary dynein in terms of a comparison with myosin and relate the results to the potentially distinguishing features of a cytoplasmic dynein.
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