Microtubule nucleation: The waltz between γ-tubulin ring complex and associated proteins
Microtubule nucleation: The waltz between γ-tubulin ring complex and associated proteins
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DOI：
10.1016/j.ceb.2020.10.004
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发表时间：
2021-02-01
影响因子：
7.5
通讯作者：
Schiebel, Elmar
中科院分区：
文献类型：
--
作者：
Liu, Peng;Wuertz, Martin;Schiebel, Elmar
微管是由ab-微管蛋白二聚体组装而成的基本细胞骨架元件。在高级真核生物中，微管成核，即微管从负端的重新组装，是由g-微管蛋白环复合物（γ - turc）启动的。尽管经过多年的研究，人们对微管成核机制的结构和机理仍然知之甚少。直到最近，低温电子显微镜研究才揭示了γ - turc的分子结构和潜在的激活机制。体外实验进一步揭示了γ - turc与其他因子（如augmin复合物、相分离蛋白TPX2和微管聚合酶XMAP215）之间的时空合作关系。这些突破加深了我们对微管成核机制的理解，并将单个微管的组装与细胞微管网络的组织联系起来。
Microtubules are essential cytoskeletal elements assembled from ab-tubulin dimers. In high eukaryotes, microtubule nucleation, the de novo assembly of a microtubule from its minus end, is initiated by the g-tubulin ring complex (gamma-TuRC). Despite many years of research, the structural and mechanistic principles of the microtubule nucleation machinery remained poorly understood. Only recently, cryoelectron microscopy studies uncovered the molecular organization and potential activation mechanisms of gamma-TuRC. In vitro assays further deciphered the spatial and temporal cooperation between gamma-TuRC and additional factors, for example, the augmin complex, the phase separation protein TPX2, and the microtubule polymerase XMAP215. These breakthroughs deepen our understanding of microtubule nucleation mechanisms and will link the assembly of individual microtubules to the organization of cellular microtubule networks.