Title |
Versatile Structures of α-Synuclein
|
---|---|
Published in |
Frontiers in Molecular Neuroscience, June 2016
|
DOI | 10.3389/fnmol.2016.00048 |
Pubmed ID | |
Authors |
Chuchu Wang, Chunyu Zhao, Dan Li, Zhiqi Tian, Ying Lai, Jiajie Diao, Cong Liu |
Abstract |
α-Synuclein (α-syn) is an intrinsically disordered protein abundantly distributed in presynaptic terminals. Aggregation of α-syn into Lewy bodies (LB) is a molecular hallmark of Parkinson's disease (PD). α-Syn features an extreme conformational diversity, which adapts to different conditions and fulfills versatile functions. However, the molecular mechanism of α-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 α-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 α-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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