Sadoul Karin, Khochbin Saadi
CNRS UMR 5309, INSERM U1209, Institut Albert Bonniot, Université Grenoble Alpes, Grenoble F-38700, France
Biochem J. 2016 Jul 1;473(13):1859-68. doi: 10.1042/BCJ20160172.
Tubulin heterodimers are the building block of microtubules, which are major elements of the cytoskeleton. Several types of post-translational modifications are found on tubulin subunits as well as on the microtubule polymer to regulate the multiple roles of microtubules. Acetylation of lysine 40 (K40) of the α-tubulin subunit is one of these post-translational modifications which has been extensively studied. We summarize the current knowledge about the structural aspects of K40 acetylation, the functional consequences, the enzymes involved and their regulation. Most importantly, we discuss the potential importance of the recently discovered additional acetylation acceptor lysines in tubulin subunits and highlight the urgent need to study tubulin acetylation in a more integrated perspective.
微管蛋白异二聚体是微管的组成成分，而微管是细胞骨架的主要成分。在微管蛋白亚基以及微管聚合物上发现了几种类型的翻译后修饰，以调节微管的多种功能。α-微管蛋白亚基赖氨酸40（K40）的乙酰化是这些翻译后修饰之一，已得到广泛研究。我们总结了目前关于K40乙酰化的结构方面、功能后果、相关酶及其调控的知识。最重要的是，我们讨论了最近在微管蛋白亚基中发现的其他乙酰化受体赖氨酸的潜在重要性，并强调迫切需要从更综合的角度研究微管蛋白乙酰化。
