Zhang Jiaming, Li Xiaoping, Li Jia-Da
Center for Reproductive Medicine, The First Affiliated Hospital, University of South China, Hengyang, China.
Hunan Key Laboratory of Animal Models for Human Diseases, School of Life Sciences, Central South University, Changsha, China.
Front Neurosci. 2019 Apr 18;13:381. doi: 10.3389/fnins.2019.00381. eCollection 2019.
Parkinson's disease is the second most common neurodegenerative disorder. Although the pathogenesis of Parkinson's disease is not entirely clear, the aberrant aggregation of α-synuclein has long been considered as an important risk factor. Elucidating the mechanisms that influence the aggregation of α-synuclein is essential for developing an effective diagnostic, preventative and therapeutic strategy to treat this devastating disease. The aggregation of α-synuclein is influenced by several post-translational modifications. Here, we summarized the major post-translational modifications (phosphorylation, ubiquitination, truncation, nitration, -GlcNAcylation) of α-synuclein and the effect of these modifications on α-synuclein aggregation, which may provide potential targets for future therapeutics.
帕金森病是第二常见的神经退行性疾病。尽管帕金森病的发病机制尚不完全清楚，但α-突触核蛋白的异常聚集长期以来一直被认为是一个重要的风险因素。阐明影响α-突触核蛋白聚集的机制对于制定有效的诊断、预防和治疗策略以治疗这种毁灭性疾病至关重要。α-突触核蛋白的聚集受几种翻译后修饰的影响。在这里，我们总结了α-突触核蛋白的主要翻译后修饰（磷酸化、泛素化、截短、硝化、O-连接N-乙酰葡糖胺化）以及这些修饰对α-突触核蛋白聚集的影响，这可能为未来的治疗提供潜在靶点。
