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Versatile Structures of α-Synuclein

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 ful...

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Autores principales: Wang, Chuchu, Zhao, Chunyu, Li, Dan, Tian, Zhiqi, Lai, Ying, Diao, Jiajie, Liu, Cong
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4913103/
https://www.ncbi.nlm.nih.gov/pubmed/27378848
http://dx.doi.org/10.3389/fnmol.2016.00048
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author Wang, Chuchu
Zhao, Chunyu
Li, Dan
Tian, Zhiqi
Lai, Ying
Diao, Jiajie
Liu, Cong
author_facet Wang, Chuchu
Zhao, Chunyu
Li, Dan
Tian, Zhiqi
Lai, Ying
Diao, Jiajie
Liu, Cong
author_sort Wang, Chuchu
collection PubMed
description 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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spelling pubmed-49131032016-07-04 Versatile Structures of α-Synuclein Wang, Chuchu Zhao, Chunyu Li, Dan Tian, Zhiqi Lai, Ying Diao, Jiajie Liu, Cong Front Mol Neurosci Neuroscience 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. Frontiers Media S.A. 2016-06-20 /pmc/articles/PMC4913103/ /pubmed/27378848 http://dx.doi.org/10.3389/fnmol.2016.00048 Text en Copyright © 2016 Wang, Zhao, Li, Tian, Lai, Diao and Liu. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution and reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Neuroscience
Wang, Chuchu
Zhao, Chunyu
Li, Dan
Tian, Zhiqi
Lai, Ying
Diao, Jiajie
Liu, Cong
Versatile Structures of α-Synuclein
title Versatile Structures of α-Synuclein
title_full Versatile Structures of α-Synuclein
title_fullStr Versatile Structures of α-Synuclein
title_full_unstemmed Versatile Structures of α-Synuclein
title_short Versatile Structures of α-Synuclein
title_sort versatile structures of α-synuclein
topic Neuroscience
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4913103/
https://www.ncbi.nlm.nih.gov/pubmed/27378848
http://dx.doi.org/10.3389/fnmol.2016.00048
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