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微管尖端相互作用蛋白:从两端看。

Microtubule tip-interacting proteins: a view from both ends.

机构信息

Department of Cell Biology, Erasmus Medical Center, P.O. Box 2040, 3000 CA Rotterdam, The Netherlands.

出版信息

Curr Opin Cell Biol. 2011 Feb;23(1):94-101. doi: 10.1016/j.ceb.2010.08.008.

DOI:10.1016/j.ceb.2010.08.008
PMID:20817499
Abstract

Microtubule ends serve as sites of tubulin addition and removal, and at the same time play crucial roles in microtubule capture, stabilization and attachment to different cellular structures. Microtubule plus and minus-ends possess distinct structural and dynamic properties, and are recognized, bound and regulated by diverse factors. These include specific capping factors such as γ-tubulin, motors, such as plus-end and minus-end directed kinesins, highly specialized kinetochore-bound microtubule-associated proteins, and comet-making plus-end tracking proteins such as EB1 and its partners. Here, we provide an overview of microtubule tip-interacting proteins and the mechanisms responsible for their association with microtubule ends, and discuss the functional cross-talk between microtubule plus and minus-end binding factors.

摘要

微管末端作为微管蛋白添加和去除的位点,同时在微管捕获、稳定和与不同细胞结构附着方面起着至关重要的作用。微管的正端和负端具有不同的结构和动态特性,并被不同的因素识别、结合和调节。这些因素包括特定的加帽因子,如γ-微管蛋白、马达,如正端和负端定向的驱动蛋白、高度专业化的着丝粒结合的微管相关蛋白,以及彗星形成的正端追踪蛋白,如 EB1 及其伴侣。在这里,我们提供了一个微管尖端相互作用蛋白的概述,以及它们与微管末端结合的机制,并讨论了微管正端和负端结合因子之间的功能交叉对话。

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