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- W4387541727 abstract "Abstract Disruption of macroautophagy/autophagy has emerged as a common feature in many neurodegenerative diseases. Autophagy is a membrane-dependent pathway that requires many key regulators to quickly localize on and off membranes during induction promoting membrane fusion. Previously, our bioinformatic approaches have shown that autophagy and Huntington disease (HD) are enriched in S-acylated proteins. S-acylation involves the reversible addition of long chain fatty acids to promote membrane binding. Herein, we show that inhibition of S-acylation regulates the abundance of several key regulators of autophagy and leads to a partial block of autophagic flux. We show that the autophagy receptor SQSTM1/p62 (sequestosome 1) is S-acylated and directed to the lysosome. Importantly, we see that SQSTM1 S-acylation is significantly reduced in HD patient and mouse model brains, thus providing a novel mechanism for the generation of empty autophagosomes previously seen in HD models and patient cells." @default.
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- W4387541727 date "2023-10-11" @default.
- W4387541727 modified "2023-10-18" @default.
- W4387541727 title "Reduced S-acylation of SQSTM1/p62 in Huntington disease is associated with impaired autophagy" @default.
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- W4387541727 doi "https://doi.org/10.1101/2023.10.11.561600" @default.
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