Regnard C, Audebert S, Boucher D, Larcher J C, Eddé B, Denoulet P
Biochimie Cellulaire, Collège de France, Paris, France.
C R Seances Soc Biol Fil. 1996;190(2-3):255-68.
In neuronal cells, microtubules are built from a very large number of alpha- and beta-tubulin variants. This diversity is due to the expression of a multigene family and to a combination of several original posttranslational modifications. Similarly, structural and motor microtubule-associated proteins, which regulate the assembly of microtubules, the modeling of their network and the mediation of their functions, are also very heterogeneous. As a consequence, mixing of these two protein polymorphisms leads to the formation of functionally-distinct microtubules. We have shown that polyglutamylation, the major posttranslational modification of neuronal tubulin, was used as a progressive regulator in the binding of structural and motor microtubule-associated proteins, in modulating gradually the conformation of the tubulin carboxy-terminal domain, playing thus a crucial role in microtubule dynamics.
在神经元细胞中,微管由大量的α-和β-微管蛋白变体构成。这种多样性源于一个多基因家族的表达以及几种原始翻译后修饰的组合。同样,调节微管组装、其网络建模及其功能介导的结构和运动微管相关蛋白也非常多样。因此,这两种蛋白质多态性的混合导致形成功能不同的微管。我们已经表明,多聚谷氨酰胺化作为神经元微管蛋白的主要翻译后修饰,在结构和运动微管相关蛋白的结合中用作渐进调节剂,逐渐调节微管蛋白羧基末端结构域的构象,从而在微管动力学中起关键作用。