帕金森病（ Parkinsons disease，PD）是目前尚无法治愈的神经系统退行性疾病，严重影响患者的生活质量。多年来，研究发现 α-突触核蛋白的过量产生或者结构异常会导致形成具有毒性作用的聚集体，这是 PD发病的关键环节。α-突触核蛋白的异常修饰与其聚集状态密切相关，如蛋白磷酸化修饰、泛素化修饰、硝基化修饰等，但这些修饰的确切作用尚不确定。近年来的研究显示乙酰化修饰在 α-突触核蛋白的异常聚集中发挥不可忽视的作用。该文就其研究进展进行综述。

Parkinsons disease (PD) is an incurable neurodegenerative disease, which seriously affects the life quality of patients. Researches in recent years found that excessive production or abnormal structure of α-synuclein and forming toxic aggregates are the key factors in the pathogenesis of PD. In a variety of mechanisms, abnormal modification of α-synuclein is closely related to its aggregation state, such as phosphorylation, ubiquitination and nitration modification, but the exact effects are still uncertain. Recent studies have shown that acetylation modification of α-synuclein plays an important role in the abnormal aggregation of α-synuclein. This article reviewed the progress of acetylation modification of α-synuclein.