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• W3202079451 abstract "Amyotrophic lateral sclerosis (ALS)-linked mutations in fused in sarcoma (FUS) lead to the formation of cytoplasmic aggregates in neurons. They are believed to play a critical role in the pathogenesis of FUS-associated ALS. Therefore, the clearance and degradation of cytoplasmic FUS aggregates in neurons may be considered a therapeutic strategy for ALS. However, the molecular pathogenic mechanisms behind FUS-associated ALS remain poorly understood. Here, we report GSK-3β as a potential modulator of FUS-induced toxicity. We demonstrated that RNAi-mediated knockdown of Drosophila ortholog Shaggy in FUS-expressing flies suppresses defective phenotypes, including retinal degeneration, motor defects, motor neuron degeneration and mitochondrial dysfunction. Furthermore, we found that cytoplasmic FUS aggregates were significantly reduced by Shaggy knockdown. In addition, we found that the levels of FUS proteins were significantly reduced by co-overexpression of Slimb, a F-box protein, in FUS-expressing flies, indicating that Slimb is critical for the suppressive effect of Shaggy/GSK-3β inhibition on FUS-induced toxicity in Drosophila. These findings revealed a novel mechanism of neuronal protective effect through SCFSlimb-mediated FUS degradation via GSK-3β inhibition, and provided in vivo evidence of the potential for modulating FUS-induced ALS progression using GSK-3β inhibitors." @default.
• W3202079451 created "2021-10-11" @default.
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• W3202079451 date "2021-10-04" @default.
• W3202079451 modified "2023-10-03" @default.
• W3202079451 title "FUS-induced neurotoxicity is prevented by inhibiting GSK-3β in a <i>Drosophila</i> model of amyotrophic lateral sclerosis" @default.
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• W3202079451 doi "https://doi.org/10.1093/hmg/ddab290" @default.
• W3202079451 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/34605896" @default.
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