Wolff A, Houdayer M, Chillet D, de Néchaud B, Denoulet P
Laboratoire de Biochimie Cellulaire, CNRS-URA 1115, Collège de France, Paris.
Biol Cell. 1994;81(1):11-6. doi: 10.1016/0248-4900(94)90049-3.
Polyglutamylation, a posttranslational modification which consists of the sequential addition of one to six glutamyl units in the carboxy-terminal domain of both tubulin subunits, is a major event in neurons. Its structure has been investigated by using monoreactive polyclonal antibodies directed against distinct glutamylation motifs, ie alpha- and gamma-linkages between glutamyl units. It is shown that, beside alpha-linkages previously characterized, gamma-linkages also occur in glutamyl chains of brain tubulin. The co-existence of these two basic motifs leads to a conception of the polyglutamyl chain with a very sophisticated structure which could, through its complexity, help the microtubule to reach its structure and fulfil its functions.
多聚谷氨酰胺化是一种翻译后修饰，它由在两个微管蛋白亚基的羧基末端结构域中依次添加一到六个谷氨酰单元组成，是神经元中的一个主要事件。其结构已通过使用针对不同谷氨酰胺化基序（即谷氨酰单元之间的α-和γ-连接）的单反应性多克隆抗体进行了研究。结果表明，除了先前已表征的α-连接外，γ-连接也存在于脑微管蛋白的谷氨酰链中。这两种基本基序的共存导致了对具有非常复杂结构的多聚谷氨酰链的一种概念，这种复杂性可能有助于微管达到其结构并履行其功能。
