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How the LLPS of \u03b1\u2010Syn is regulated remains largely unknown. Here, we discovered that the C\u2010terminal region modulates \u03b1\u2010Syn phase separation through electrostatic interactions. The wild\u2010type (WT) and PD disease\u2010related truncated \u03b1\u2010Syn can co\u2010exist in the condensates. The truncated \u03b1\u2010Syn could dramatically promote WT \u03b1\u2010Syn phase separation. Further studies demonstrated that the truncated \u03b1\u2010Syn accelerated WT \u03b1\u2010Syn turning to amyloid aggregates by modulation of phase separation. Together, our findings disclose the role of the C\u2010terminal domain in the LLPS of \u03b1\u2010Syn and pave the path for understanding the mechanism of truncated \u03b1\u2010Syn in PD pathology.<\/jats:p>","DOI":"10.1002\/1873-3468.14361","type":"journal-article","created":{"date-parts":[[2022,4,29]],"date-time":"2022-04-29T14:07:33Z","timestamp":1651241253000},"page":"1388-1400","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":49,"title":["\u03b1\u2010Synuclein phase separation and amyloid aggregation are modulated by C\u2010terminal truncations"],"prefix":"10.1002","volume":"596","author":[{"given":"Shuai","family":"Huang","sequence":"first","affiliation":[{"name":"Jiangsu Key Laboratory for Molecular and Medical Biotechnology College of Life Sciences Nanjing Normal University  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