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Microtubule tip-interacting proteins: a view from both ends

机译:微管末端相互作用蛋白:两端视图

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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 gamma-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.
机译:微管末端是微管蛋白添加和去除的位点,同时在微管捕获,稳定化和附着于不同细胞结构中起关键作用。微管的正负两端具有独特的结构和动态特性,并受到各种因素的识别,约束和调节。这些包括特定的加帽因子,例如γ-微管蛋白,马达(例如正向和负向定向的驱动蛋白),高度专业化的受线粒结合的微管相关蛋白,以及彗星制造的正向跟踪蛋白(例如EB1及其合作伙伴) 。在这里,我们提供了微管末端相互作用蛋白及其与微管末端相关联的机制的概述,并讨论了微管正负结合因子之间的功能串扰。

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