文章基本信息

标题：The Mechanism of Tubulin Assembly into Microtubules: Insights from Structural Studies
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作者：Marcel Knossow ; Valérie Campanacci ; Liza Ammar Khodja 等
期刊名称：iScience
印刷版ISSN：2589-0042
出版年度：2020
卷号：23
期号：9
页码：1-14
DOI：10.1016/j.isci.2020.101511
语种：English
出版社：Elsevier
摘要：SummaryMicrotubules are cytoskeletal components involved in pivotal eukaryotic functions such as cell division, ciliogenesis, and intracellular trafficking. They assemble from αβ-tubulin heterodimers and disassemble in a process called dynamic instability, which is driven by GTP hydrolysis. Structures of the microtubule and of soluble tubulin have been determined by cryo-EM and by X-ray crystallography, respectively. Altogether, these data define the mechanism of tubulin assembly-disassembly at atomic or near-atomic level. We review here the structural changes that occur during assembly, tubulin switching from a curved conformation in solution to a straight one in the microtubule core. We also present more subtle changes associated with GTP binding, leading to tubulin activation for assembly. Finally, we show how cryo-EM and X-ray crystallography are complementary methods to characterize the interaction of tubulin with proteins involved either in intracellular transport or in microtubule dynamics regulation.Graphical AbstractDisplay OmittedBiochemistry Methods, Cell Biology, Structural Biology