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动力蛋白重链异构体与轴丝运动性。

Dynein heavy chain isoforms and axonemal motility.

作者信息

Asai D J, Brokaw C J

机构信息

Department of Biological Sciences, Purdue University, West Lafayette, IN 47907, USA.

出版信息

Trends Cell Biol. 1993 Nov;3(11):398-402. doi: 10.1016/0962-8924(93)90090-n.

Abstract

The translocation of dynein along microtubules is the basis for a wide variety of essential cellular movements. Dynein was first discovered in the ciliary axoneme, where it causes the directed sliding between outer doublet microtubules that underlies ciliary bending. The initiation and propagation of ciliary bends are produced by a precisely located array of different dyneins containing eight or more different dynein heavy chain isoforms. The detailed clarification of the structural and functional diversity of axonemal dynein heavy chains will not only provide the key to understanding how cilia function, but also give insights applicable to the study of non-axonemal microtubule motors.

摘要

动力蛋白沿微管的易位是多种基本细胞运动的基础。动力蛋白最初是在纤毛轴丝中发现的,它在那里导致外双联微管之间的定向滑动,这是纤毛弯曲的基础。纤毛弯曲的起始和传播是由一系列精确定位的不同动力蛋白产生的,这些动力蛋白包含八种或更多不同的动力蛋白重链异构体。对轴丝动力蛋白重链的结构和功能多样性的详细阐明,不仅将为理解纤毛如何发挥功能提供关键,还将为非轴丝微管马达的研究提供适用的见解。

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