Structural switching of tubulin in the microtubule lattice.

IF 4.3 3区 生物学 Q2 BIOCHEMISTRY & MOLECULAR BIOLOGY
Yean-Ming Chew, Robert A Cross
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引用次数: 0

Abstract

Microtubule (MT) dynamic instability, a cycle of growth, catastrophe, shrinkage and rescue, is driven by the switching of tubulin between two structural states, one stabilised by GTP and the other by GDP. Recent work has uncovered the ancient origins of this structural switch and revealed further fundamental elements of microtubule dynamic instability, whereby switching can be brought about by a range of allosteric effectors, propagate deep within the lattice of assembled MTs, and profoundly affect MT function. Here, we review evidence for structural switching within the MT lattice and discuss current ideas about its mechanisms.

微管晶格中微管蛋白的结构开关。
微管(MT)的动态不稳定性是由微管蛋白在两种结构状态之间的切换驱动的,一种由GTP稳定,另一种由GDP稳定。最近的工作揭示了这种结构开关的古老起源,并进一步揭示了微管动态不稳定性的基本要素,即开关可以由一系列变构效应物引起,在组装的MT晶格内深入传播,并深刻影响MT功能。在这里,我们回顾了MT晶格内结构转换的证据,并讨论了目前关于其机制的想法。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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来源期刊
Biochemical Society transactions
Biochemical Society transactions 生物-生化与分子生物学
CiteScore
7.80
自引率
0.00%
发文量
351
审稿时长
3-6 weeks
期刊介绍: Biochemical Society Transactions is the reviews journal of the Biochemical Society. Publishing concise reviews written by experts in the field, providing a timely snapshot of the latest developments across all areas of the molecular and cellular biosciences. Elevating our authors’ ideas and expertise, each review includes a perspectives section where authors offer comment on the latest advances, a glimpse of future challenges and highlighting the importance of associated research areas in far broader contexts.
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