Role of glutathione transferase in phase separation of FUS and TAF15 in neurons  

作　　者：Kiyoung Kim 

机构地区：[1]Department of Medical Science,Soonchunhyang University,Asan,Korea

出　　处：《Neural Regeneration Research》2025年第7期1999-2000,共2页中国神经再生研究（英文版）

基　　金：supported by the BK21 FOUR(Fostering Outstanding Universities for Research)and the Basic Science Research Program through the National Research Foundation of Korea(NRF),funded by the Ministry of Education(MOE)and the Ministry of Science and ICT(MSIT)(NRF-2022R1A2C1004204,RS-2023-00219563,2023-DD-UP-0007);by the Soonchunhyang University Research Fund(to KK)。

摘　　要：Amyotrophic lateral sclerosis(ALS)is a progressive neurodegenerative disorder characterized by the degeneration of motor neurons in the brain and spinal cord,leading to muscle weakness,paralysis,and ultimately death(Cleveland and Rothstein,2001).Frontotemporal lobar degeneration(FTLD)is a neurodegenerative disease affecting the frontal and temporal lobes of the brain,leading to changes in behavior,personality,and language(Van Langenhove et al.,2012).Both ALS and FTLD are classified as proteinopathies in which abnormal protein aggregation and accumulation in neurons contribute to the disease pathogenesis.Fused in sarcoma(FUS)is a DNA/RNA-binding protein involved in various cellular processes,including transcriptional regulation,RNA splicing,and DNA repair.Mutations in the FUS gene have been linked to familial ALS,highlighting the importance of FUS in the disease pathogenesis(Vance et al.,2009).In ALS and FTLD,aberrant post-translational modifications(PTMs)of FUS,such as phosphorylation,acetylation,and methylation,have been implicated in the promotion of FUS aggregation and neurotoxicity(Choi et al.,2023).Therefore,understanding the regulatory mechanisms of FUS PTMs is crucial for developing targeted therapies against these diseases.

关 键 词：DEGENERATION FUS AGGREGATION 

分 类 号：R744.8[医药卫生—神经病学与精神病学]