Journal
TRENDS IN BIOCHEMICAL SCIENCES
Volume 43, Issue 11, Pages 921-932Publisher
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tibs.2018.07.002
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Funding
- Medical Research Council UK [MC_ U105663142, MC_ U105674181]
- Wellcome Trust Investigator award [110159/Z/15/Z]
- Research Foundation - Flanders (FWO)
- European Union's Horizon 2020 research and innovation programme under the Marie Sklodowska-Curie grant [665501]
- Fonds Wetenschappelijk Onderzoek-Vlaanderen [1.5.193.18N]
- MRC [MC_U105663142, MC_U105674181, MC_UU_00015/3] Funding Source: UKRI
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Thousands of protein acyl modification sites have now been identified in vivo. However, at most sites the acylation stoichiometry is low, making functional enzyme-driven regulation in the majority of cases unlikely. As unmediated acylation can occur on the surface of proteins when acyl-CoA thioesters react with nucleophilic cysteine and lysine residues, slower nonenzymatic processes likely underlie most protein acylation. Here, we review how nonenzymatic acylation of nucleophilic lysine and cysteine residues occurs; the factors that enhance acylation at particular sites; and the strategies that have evolved to limit protein acylation. We conclude that protein acylation is an unavoidable consequence of the central role of reactive thioesters in metabolism. Finally, we propose a hypothesis for why low-stoichiometry protein acylation is selected against by evolution and how it might contribute to degenerative processes such as aging.
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