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Review explores the role of S-palmitoylation in regulating proteins and its implications for health and disease.
S-palmitoylation is a reversible protein post-translational modification whereby a 16C fatty acid chain is attached to a cysteine residue via a thioester bond. This modification is crucial in regulating protein localization, conformation, stability, and interaction with other molecules. It influences multifarious physiological functions, from immune signaling to cellular apoptosis. In recent years, protein palmitoylation and diverse disease pathogenesis have been increasingly linked; this review intends to present a recent overview of the area, covering its catalysis mechanisms, functional significance, and role in diseases while discussing research challenges to strengthen our understanding of S-palmitoylation. Rather than providing an exhaustive summary, this review focuses on specific recent exemplars to illustrate the biological importance of S-acylation.
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Wong et al. (2026) studied this question.
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