School of Biology, IISER Thiruvananthapuram, Thiruvananthapuram, Kerala, India.
School of Biology, IISER Thiruvananthapuram, Thiruvananthapuram, Kerala, India.
Methods Cell Biol. 2022;169:43-66. doi: 10.1016/bs.mcb.2021.12.002. Epub 2022 Feb 24.
Alpha-synuclein (α-syn) is a natively unfolded protein that is abundantly expressed in the central nervous system. Although it has been shown to be involved in neurotransmission and cognition, its exact functions remain elusive. The misfolding of this protein into β-sheet-rich amyloid structures and subsequent aggregation has been associated with several neurodegenerative diseases, including Parkinson's disease. The interaction of α-syn with lipid membranes has been implicated in the formation of these pathological aggregates. At the same time, some physiological functions of α-syn also seem to require membrane interactions. A majority of the disease-associated mutations of α-syn occur in the lipid binding domain, further indicating the importance of membrane interactions in health and disease. A comprehensive understanding of the factors that modulate these interactions will help delineate the physiological and pathological states of this protein.
α-突触核蛋白（α-syn）是一种天然无规则卷曲的蛋白质，在中枢神经系统中大量表达。尽管它已被证明参与神经传递和认知过程，但确切功能仍不清楚。该蛋白错误折叠成富含β-折叠的淀粉样结构并随后聚集，与包括帕金森病在内的几种神经退行性疾病有关。α-syn 与脂膜的相互作用与这些病理性聚集物的形成有关。同时，α-syn 的一些生理功能似乎也需要膜相互作用。大多数与疾病相关的 α-syn 突变发生在脂结合域，进一步表明膜相互作用在健康和疾病中的重要性。全面了解调节这些相互作用的因素将有助于描绘该蛋白的生理和病理状态。
