Wloga Dorota, Joachimiak Ewa, Louka Panagiota, Gaertig Jacek
Laboratory of Cytoskeleton and Cilia Biology, Department of Cell Biology, Nencki Institute of Experimental Biology, Polish Academy of Sciences, 02-093 Warsaw, Poland.
Department of Cellular Biology, University of Georgia, Athens, Georgia 30602.
Cold Spring Harb Perspect Biol. 2017 Jun 1;9(6):a028159. doi: 10.1101/cshperspect.a028159.
Tubulin undergoes several highly conserved posttranslational modifications (PTMs) including acetylation, detyrosination, glutamylation, and glycylation. These PTMs accumulate on a subset of microtubules that are long-lived, including those in the basal bodies and axonemes. Tubulin PTMs are distributed nonuniformly. In the outer doublet microtubules of the axoneme, the B-tubules are highly enriched in the detyrosinated, polyglutamylated, and polyglycylated tubulin, whereas the A-tubules contain mostly unmodified tubulin. The nonuniform patterns of tubulin PTMs may functionalize microtubules in a position-dependent manner. Recent studies indicate that tubulin PTMs contribute to the assembly, disassembly, maintenance, and motility of cilia. In particular, tubulin glutamylation has emerged as a key PTM that affects ciliary motility through regulation of axonemal dynein arms and controls the stability and length of the axoneme.
微管蛋白经历多种高度保守的翻译后修饰(PTM),包括乙酰化、去酪氨酸化、谷氨酰胺化和甘氨酰化。这些PTM积累在长寿微管的一个子集上,包括基体和轴丝中的微管。微管蛋白PTM分布不均匀。在轴丝的外双联微管中,B微管富含去酪氨酸化、多聚谷氨酰胺化和多聚甘氨酰化的微管蛋白,而A微管主要含有未修饰的微管蛋白。微管蛋白PTM的不均匀模式可能以位置依赖的方式使微管发挥功能。最近的研究表明,微管蛋白PTM有助于纤毛的组装、拆卸、维持和运动。特别是,微管蛋白谷氨酰胺化已成为一种关键的PTM,它通过调节轴丝动力蛋白臂来影响纤毛运动,并控制轴丝的稳定性和长度。