Axoneme Structure from Motile Cilia

Axoneme Structure from Motile Cilia
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DOI:
10.1101/cshperspect.a028076
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发表时间:
2017-01-01
影响因子:
7.2
通讯作者:
Ishikawa, Takashi
Ishikawa, Takashi
中科院分区:
生物学1区
文献类型:
--
作者:
Ishikawa, Takashi

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轴丝是真核生物纤毛和鞭毛的主要胞外部分。它由一个微管细胞骨架组成,通常由九个双峰组成。在运动纤毛中,动力蛋白ATP酶马达蛋白在相邻的微管之间产生滑动运动,这些运动被整合成一种精心编排的跳动或旋转运动。在初级纤毛中,有许多感觉蛋白在轴丝周围的膜上起作用。在这两种情况下,正如蛋白质组学研究所阐明的那样,数百种蛋白质存在于这种分隔的生物分子系统中。本文综述了近年来利用电子显微镜和X射线晶体学对轴丝及其组成部分结构的研究进展,主要集中在运动纤毛方面。结构生物学提供动态结构变化的快照(但不是实时成像),并深入了解动力蛋白的力产生机制,纤毛弯曲机制,纤毛发生和轴丝的进化。
The axoneme is the main extracellular part of cilia and flagella in eukaryotes. It consists of a microtubule cytoskeleton, which normally comprises nine doublets. In motile cilia, dynein ATPase motor proteins generate sliding motions between adjacent microtubules, which are integrated into a well-orchestrated beating or rotational motion. In primary cilia, there are a number of sensory proteins functioning on membranes surrounding the axoneme. In both cases, as the study of proteomics has elucidated, hundreds of proteins exist in this compartmentalized biomolecular system. In this article, we review the recent progress of structural studies of the axoneme and its components using electron microscopy and X-ray crystallography, mainly focusing on motile cilia. Structural biology presents snapshots (but not live imaging) of dynamic structural change and gives insights into the force generation mechanism of dynein, ciliary bending mechanism, ciliogenesis, and evolution of the axoneme.