The SMN complex, an assemblyosome of ribonucleoproteins
The SMN complex, an assemblyosome of ribonucleoproteins
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DOI：
10.1016/s0955-0674(02)00332-0
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发表时间：
2002-06-01
影响因子：
7.5
通讯作者：
Dreyfuss, G
中科院分区：
文献类型：
--
作者：
Paushkin, S;Gubitz, AK;Dreyfuss, G
脊髓性肌萎缩症是一种常见的、通常是致命的神经退行性疾病，由运动神经元存活蛋白（SMN）的低水平或功能突变丧失引起。SMN寡聚并与另外五种蛋白质形成稳定的复合物：Gemins 2-6。SMN还与其他几种称为“底物”的蛋白质相互作用。这些底物大多含有一个富含精氨酸和甘氨酸残基的结构域（RG-rich domain），是不同核糖核蛋白复合物的组成部分。最近的研究表明，底物可以通过精氨酸甲基转移酶复合物（甲基体）进行修饰。这在底物富含rg的区域内形成对称的二甲基精氨酸，从而将它们转化为SMN复合物的高亲和力结合物，并且很可能提供核糖核蛋白组装过程的调节。
Spinal muscular atrophy is a common, often lethal, neurodegenerative disease that results from low levels of, or loss-of-function mutations in, the SMN (survival of motor neurons) protein. SMN oligomerizes and forms a stable complex with five additional proteins: Gemins 2-6. SMN also interacts with several additional proteins referred to as 'substrates'. Most of these substrates contain a domain enriched in arginine and glycine residues (the RG-rich domain), and are constituents of different ribonucleoprotein complexes. Recent studies revealed that the substrates can be modified by an arginine methyltransferase complex, the methylosome. This forms symmetrical dimethylarginines within the RG-rich domains of the substrates, thereby converting them to high-affinity binders of the SMN complex, and most likely providing regulation of the ribonucleoprotein assembly processes.