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秀丽隐杆线虫中的微管蛋白。

Tubulins in C. elegans.

作者信息

Hurd Daryl D

机构信息

Biology Department, St. John Fisher College, Rochester, NY 14618 USA.

出版信息

WormBook. 2018 Aug 4;2018:1-32. doi: 10.1895/wormbook.1.182.1.

Abstract

The C. elegans tubulin family is composed of nine α-, six β-, and one γ-tubulin. Tubulins are highly conserved, functioning as α-β heterodimers that assemble into microtubules. These cylindrical and ubiquitous components of the cytoskeleton are critical for nearly all cellular and developmental processes. C. elegans has provided a model for the study of microtubules in multiple settings including separation of chromosomes, cellular polarity, and neuronal sensation. Tubulins and microtubules interact with a long list of other cellular proteins that regulate tubulin homeostasis, modify microtubule dynamics, and control incorporation into or disassociation of higher-order cellular structures such as spindles or ciliary axonemes. A collection of enzymes modifies tubulins, often at the variable carboxyl-terminal tail, adding another layer of regulation to microtubule structure and function. Genetic and cytological studies in C. elegans have revealed roles for tubulin and its associated proteins in numerous contexts from embryogenesis to adult behavior.

摘要

秀丽隐杆线虫的微管蛋白家族由9种α-微管蛋白、6种β-微管蛋白和1种γ-微管蛋白组成。微管蛋白高度保守,以α-β异二聚体的形式发挥作用,组装成微管。这些细胞骨架中呈圆柱形且普遍存在的成分对几乎所有细胞和发育过程都至关重要。秀丽隐杆线虫为在多种情况下研究微管提供了一个模型,这些情况包括染色体分离、细胞极性和神经元感知。微管蛋白和微管与一长串其他细胞蛋白相互作用,这些蛋白调节微管蛋白稳态、改变微管动力学,并控制其并入或脱离诸如纺锤体或纤毛轴丝等高阶细胞结构。一系列酶会修饰微管蛋白,通常是在可变的羧基末端尾部,为微管的结构和功能增添了另一层调控。秀丽隐杆线虫的遗传学和细胞学研究揭示了微管蛋白及其相关蛋白在从胚胎发生到成虫行为的众多情况下所起的作用。

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