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- W2993137128 endingPage "118620" @default.
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- W2993137128 abstract "Protein S-palmitoylation, the covalent lipid modification of the side chain of Cys residues with the 16‑carbon fatty acid palmitate, is the most common acylation, and it enhances the membrane stability of ion channels. This post-translational modification (PTM) determines a functional mechanism of ion channel life cycle from maturation and membrane trafficking to localization. Especially, neurodevelopment is regulated by balancing the level of synaptic protein palmitoylation/depalmitoylation. Recently, we revealed the pathological role of the transient receptor potential canonical type 5 (TRPC5) channel in striatal neuronal loss during Huntington's disease (HD), which is abnormally activated by oxidative stress. Here, we report a mechanism of TRPC5 palmitoylation at a conserved cysteine residue, that is critical for intrinsic channel activity. Furthermore, we identified the therapeutic effect of TRPC5 depalmitoylation by enhancing the TRPC5 membrane instability on HD striatal cells in order to lower TRPC5 toxicity. Collectively, these findings suggest that controlling S-palmitoylation of the TRPC5 channel as a potential risk factor can modulate TRPC5 channel expression and activity, providing new insights into a therapeutic strategy for neurodegenerative diseases." @default.
- W2993137128 created "2019-12-13" @default.
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- W2993137128 date "2020-02-01" @default.
- W2993137128 modified "2023-09-25" @default.
- W2993137128 title "TRPC5 channel instability induced by depalmitoylation protects striatal neurons against oxidative stress in Huntington's disease" @default.
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- W2993137128 doi "https://doi.org/10.1016/j.bbamcr.2019.118620" @default.
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