title: Versatile Structures of α-Synuclein.
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.
authors.affiliation: Interdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences Shanghai, China.
authors.forename: Chuchu
authors.initials: C
authors.lastname: Wang
authors.affiliation: Interdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences Shanghai, China.
authors.forename: Chunyu
authors.initials: C
authors.lastname: Zhao
authors.affiliation: Interdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences Shanghai, China.
authors.forename: Dan
authors.initials: D
authors.lastname: Li
authors.affiliation: Department of Cancer Biology, College of Medicine, University of CincinnatiCincinnati, OH, USA; Center for Mitochondrial Biology and Medicine, Key Laboratory of Biomedical Information Engineering of Ministry of the Education School of Life Science, Xi'an Jiaotong UniversityXi'an, China.
authors.forename: Zhiqi
authors.initials: Z
authors.lastname: Tian
authors.affiliation: Department of Molecular and Cellular Physiology, Stanford University Stanford, CA, USA.
authors.forename: Ying
authors.initials: Y
authors.lastname: Lai
authors.affiliation: Department of Cancer Biology, College of Medicine, University of Cincinnati Cincinnati, OH, USA.
authors.forename: Jiajie
authors.initials: J
authors.lastname: Diao
authors.affiliation: Interdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences Shanghai, China.
authors.forename: Cong
authors.initials: C
authors.lastname: Liu
keywords: Parkinson’s disease; amyloid; atomic structure; protein aggregation; vesicle trafficking; α-synuclein