Tofaris G K, Spillantini M G
Cambridge Centre for Brain Repair and Department of Clinical Neuroscience Forvie Site, Robinson Way, Cambridge CB2 2PY, United Kingdom.
Cell Mol Life Sci. 2007 Sep;64(17):2194-201. doi: 10.1007/s00018-007-7217-5.
alpha-Synuclein belongs to a small group of natively unfolded proteins that can transiently bind to lipid membranes and acquire a partial alpha-helical conformation. Under certain pathogenic conditions, alpha-synuclein aggregates to form oligomers and insoluble fibrils with increased ss-sheet configuration. Although genetic mutations and multiplications of the gene have been found in familial cases, the mechanism by which this protein aggregates in sporadic cases of Parkinson's disease, dementia with Lewy bodies and multisystem atrophy is not fully understood. Here we review the function of alpha-synuclein and recent insight into the mechanisms by which it aggregates.
α-突触核蛋白属于一小类天然未折叠蛋白,它们可以短暂地与脂质膜结合并获得部分α-螺旋构象。在某些致病条件下,α-突触核蛋白会聚集形成具有增加的β-折叠结构的寡聚体和不溶性纤维。虽然在家族性病例中发现了该基因的突变和倍增,但这种蛋白在散发性帕金森病、路易体痴呆和多系统萎缩病例中聚集的机制尚未完全了解。在这里,我们综述了α-突触核蛋白的功能以及对其聚集机制的最新见解。