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肌萎缩侧索硬化症(amyotrophic lateral sclerosis,ALS)是一种以运动神经细胞死亡为特征的、致命性神经退行性疾病。作为一种RNA结合蛋白,肉瘤融合蛋白(fused in sarcoma,FUS)突变引起ALS。应激颗粒(stress granules,SG)是细胞在应激条件下产生的细胞质结构。FUS存在于SG中,SG标记物是FUS阳性聚集体的组分,提示FUS突变体可能干扰SG正常功能,并且SG可能作为病理性FUS聚集体的前体。该文探讨了SG募集FUS的机制与调控,分析了SG与FUS聚集体之间的关系,以期为了解SG在FUS突变引起的ALS发生中的作用提供参考。
Amyotrophic lateral sclerosis (ALS) is a fatal neurodegenerative disease characterized by motor nerve cell death. As an RNA-binding protein, mutations in the fused in sarcoma (FUS) cause ALS. Stress granules (SG) are the cytoplasmic structures that cells produce under stress conditions. FUS is present in SG and SG markers are components of FUS-positive aggregates, suggesting that FUS mutants may interfere with the normal function of SG and that SG may serve as a precursor for pathological FUS aggregates. This paper explored the mechanism and regulation of FUS mobilization by SG and analyzed the relationship between SG and FUS aggregates in order to provide a reference for understanding the role of SG in the pathogenesis of ALS caused by FUS mutation.