Savyon Mor, Engelender Simone
Department of Biochemistry, The B. Rappaport Faculty of Medicine and Institute of Medical Research, Technion - Israel Institute of Technology, Haifa, Israel.
Front Aging Neurosci. 2020 Jun 25;12:167. doi: 10.3389/fnagi.2020.00167. eCollection 2020.
The accumulation and aggregation of α-synuclein are central to Parkinson's disease (PD), yet the molecular mechanisms responsible for these events are not fully understood. Post-translational modifications of α-synuclein regulate several of its properties, including degradation, interaction with proteins and membranes, aggregation and toxicity. SUMOylation is a post-translational modification involved in various nuclear and extranuclear processes, such as subcellular protein targeting, mitochondrial fission and synaptic plasticity. Protein SUMOylation increases in response to several stressful situations, from viral infections to trauma. In this framework, an increasing amount of evidence has implicated SUMOylation in several neurodegenerative diseases, including PD. This review will discuss recent findings in the role of SUMOylation as a regulator of α-synuclein accumulation, aggregation and toxicity, and its possible implication in neurodegeneration that underlies PD.
α-突触核蛋白的积累和聚集是帕金森病（PD）的核心问题，然而导致这些事件的分子机制尚未完全明确。α-突触核蛋白的翻译后修饰调节其多种特性，包括降解、与蛋白质及膜的相互作用、聚集和毒性。小泛素样修饰（SUMOylation）是一种参与各种核内和核外过程的翻译后修饰，如亚细胞蛋白质靶向、线粒体分裂和突触可塑性。从病毒感染到创伤等多种应激情况下，蛋白质的SUMOylation都会增加。在此背景下，越来越多的证据表明SUMOylation与包括PD在内的几种神经退行性疾病有关。本综述将讨论SUMOylation作为α-突触核蛋白积累、聚集和毒性调节剂的最新研究结果，及其在PD潜在神经退行性变中的可能作用。
