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Therapeutic modulation of GSTO activity rescues FUS-associated neurotoxicity via deglutathionylation in ALS disease models
- Authors
- Cha, Sun Joo; Lee, Seongsoo; Choi, Hyun-Jun; Han, Yeo Jeong; Jeon, Yu-Mi; Jo, Myungjin; Lee, Shinrye; Nahm, Minyeop; Lim, Su Min; Kim, Seung Hyun; Kim Hyung-Jun; Kim, Kiyoung
- Issue Date
- Mar-2022
- Publisher
- Cell Press
- Citation
- Developmental Cell, v.57, no.6, pp.783 - 798.e8
- Journal Title
- Developmental Cell
- Volume
- 57
- Number
- 6
- Start Page
- 783
- End Page
- 798.e8
- ISSN
- 1534-5807
- Abstract
- Fused in sarcoma (FUS) is a DNA/RNA-binding protein that is involved in DNA repair and RNA processing. FUS is associated with neurodegenerative diseases such as amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD). However, the molecular mechanisms underlying FUS-mediated neurodegeneration are largely unknown. Here, using a Drosophila model, we showed that the overexpression of glutathione transferase omega 2 (GstO2) reduces cytoplasmic FUS aggregates and prevents neurodegenerative phenotypes, including neurotoxicity and mitochondrial dysfunction. We found a FUS glutathionylation site at the 447
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