Kubo Tomohiro, Oda Toshiyuki
Department of Anatomy and Structural Biology, Graduate School of Medicine, University of Yamanashi, Shimokato, Chuo, Yamanashi, Japan.
Microscopy (Oxf). 2019 Feb 1;68(1):80-91. doi: 10.1093/jmicro/dfy044.
The diversity of α- and β-tubulin is facilitated by various post-translational modifications (PTMs), such as acetylation, tyrosination, glycylation, glutamylation, phosphorylation and methylation. These PTMs affect the stability and structure of microtubules as well as the interaction between microtubules and microtubule-associated proteins, including molecular motors. Therefore, it is extremely important to investigate the roles of tubulin PTMs for understanding the cell cycle, cell motility and intracellular trafficking. Tubulin PTMs were first studied in the 1980s, and considerable progress has been made since then; it is likely that additional mechanisms remain yet to be elucidated. Here, we discuss one such modification, tubulin glutamylation, and introduce our research on the eukaryotic flagellum of the unicellular green alga Chlamydomonas reinhardtii.
α-微管蛋白和β-微管蛋白的多样性是由多种翻译后修饰（PTM）促成的，如乙酰化、酪氨酰化、甘氨酰化、谷氨酰化、磷酸化和甲基化。这些翻译后修饰会影响微管的稳定性和结构，以及微管与微管相关蛋白（包括分子马达）之间的相互作用。因此，研究微管蛋白翻译后修饰对于理解细胞周期、细胞运动和细胞内运输的作用极其重要。微管蛋白翻译后修饰最早是在20世纪80年代进行研究的，从那时起已经取得了相当大的进展；很可能还有其他机制有待阐明。在这里，我们讨论一种这样的修饰——微管蛋白谷氨酰化，并介绍我们对单细胞绿藻莱茵衣藻真核鞭毛的研究。
