期刊
FRONTIERS IN MOLECULAR NEUROSCIENCE
卷 9, 期 -, 页码 -出版社
FRONTIERS MEDIA SA
DOI: 10.3389/fnmol.2016.00048
关键词
alpha-synuclein; Parkinson's disease; amyloid; atomic structure; vesicle trafficking; protein aggregation
资金
- 1000 Talents Program of China
- State High-Tech Development Plan (the 863 Program) [2015AA020907]
- National Natural Science Foundation (NSF) of China [31470748]
- 973-program [2015CB856304]
alpha-Synuclein (alpha-syn) is an intrinsically disordered protein abundantly distributed in presynaptic terminals. Aggregation of alpha-syn into Lewy bodies (LB) is a molecular hallmark of Parkinson's disease (PD). alpha-Syn features an extreme conformational diversity, which adapts to different conditions and fulfills versatile functions. However, the molecular mechanism of alpha-syn transformation and the relation between different structural species and their functional and pathogenic roles in neuronal activities and PD remain unknown. In this mini-review, we summarize the recent discoveries of alpha-syn structures in the membrane-bound state, in cytosol, and in the amyloid state under physiological and pathological conditions. From the current knowledge on different structural species of alpha-syn, we intend to find a clue about its function and toxicity in normal neurons and under disease conditions, which could shed light on the PD pathogenesis.
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