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Meanwhile, post-translational modifications (PTMs) of \u03b1-syn such as acetylation and phosphorylation play important yet distinct roles in regulating \u03b1-syn conformation, membrane binding, and amyloid aggregation. However, how PTMs regulate \u03b1-syn function in presynaptic terminals remains unclear. Here, based on our previous findings, we further demonstrate that N-terminal acetylation, which occurs under physiological conditions and is irreversible in mammalian cells, significantly enhances the functional activity of \u03b1-syn in clustering SVs. Mechanistic studies reveal that this enhancement is caused by the N-acetylation-promoted insertion of \u03b1-syn\u2019s N-terminus and increased intermolecular interactions on the LPC-containing membrane. N-acetylation in our work is shown to fine-tune the interaction between \u03b1-syn and LPC, mediating \u03b1-syn\u2019s role in synaptic vesicle clustering.<\/jats:p>","DOI":"10.7554\/elife.97228","type":"journal-article","created":{"date-parts":[[2024,4,19]],"date-time":"2024-04-19T07:25:50Z","timestamp":1713511550000},"update-policy":"https:\/\/doi.org\/10.7554\/elife.97228","source":"Crossref","is-referenced-by-count":9,"title":["N-acetylation of \u03b1-synuclein enhances synaptic vesicle clustering mediated by \u03b1-synuclein and lysophosphatidylcholine"],"prefix":"10.7554","volume":"13","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-2015-7331","authenticated-orcid":true,"given":"Chuchu","family":"Wang","sequence":"first","affiliation":[{"id":[{"id":"https:\/\/ror.org\/01y3hvq34","id-type":"ROR","asserted-by":"publisher"}],"name":"Interdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of 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