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首页> 外文期刊>International Journal of Neuroscience >Protein SUMOylation, an emerging pathway in amyotrophic lateral sclerosis
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Protein SUMOylation, an emerging pathway in amyotrophic lateral sclerosis

机译：蛋白质SUMOylation，肌萎缩性侧索硬化症的新兴途径

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摘要

The covalent attachment of SUMO proteins (small ubiquitin-like modifier) to specific proteins or SUMOylation regulates their functional properties in the nucleus and cytoplasm of neurons. Recent studies reported dysfunction of the SUMO pathway in molecular and cellular abnormalities associated with amyotrophic lateral sclerosis (ALS). Furthermore, several observations support a direct role for SUMOylation in diverse pathogenic mechanisms involved in ALS, such as response to hypoxia, oxidative stress, glutamate excitotoxicity and proteasome impairment. Recent results also suggest that SUMO modifications of superoxide dismutase 1, transactive response DNA-binding protein 43, CTE (COOH terminus of EAAT2) (proteolytic C-terminal fragment of the glutamate transporter excitatory amino acid transporter 2, EAAT2) and proteins regulating the turnover of ALS-related proteins can participate in the pathogenesis of ALS. Moreover, the fused in sarcoma (FUS) gene, mutated in ALS, encodes a protein with a SUMO E3 ligase activity. In this review, we summarize the functioning of the SUMO pathway in normal conditions and in response to stresses, its action on ALS-related proteins and discuss the need for further research on this pathway in ALS.
机译：SUMO蛋白（小的泛素样修饰剂）与特定蛋白的共价连接或SUMOylation调节其在神经元细胞核和细胞质中的功能特性。最近的研究报道了在与肌萎缩性侧索硬化症（ALS）相关的分子和细胞异常中SUMO途径的功能障碍。此外，一些观察结果支持SUMOylation在涉及ALS的多种致病机制中的直接作用，例如对缺氧，氧化应激，谷氨酸兴奋性毒性和蛋白酶体损伤的反应。最近的结果还表明，SUMO修饰了超氧化物歧化酶1，交易反应DNA结合蛋白43，CTE（EAAT2的COOH末端）（谷氨酸转运蛋白兴奋性氨基酸转运蛋白2的蛋白水解C末端片段，EAAT2）和调节营业额的蛋白ALS相关蛋白中的一部分可以参与ALS的发病。此外，在ALS中发生突变的融合肉瘤（FUS）基因编码具有SUMO E3连接酶活性的蛋白质。在这篇综述中，我们总结了SUMO途径在正常情况下的功能以及对压力的反应及其对ALS相关蛋白的作用，并讨论了在ALS中对该途径进行进一步研究的必要性。

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