Unknown

Dataset Information

0

Versatile Structures of ?-Synuclein.


ABSTRACT: ?-Synuclein (?-syn) is an intrinsically disordered protein abundantly distributed in presynaptic terminals. Aggregation of ?-syn into Lewy bodies (LB) is a molecular hallmark of Parkinson's disease (PD). ?-Syn features an extreme conformational diversity, which adapts to different conditions and fulfills versatile functions. However, the molecular mechanism of ?-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 ?-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 ?-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.

SUBMITTER: Wang C 

PROVIDER: S-EPMC4913103 | biostudies-literature | 2016

REPOSITORIES: biostudies-literature

altmetric image

Publications

Versatile Structures of α-Synuclein.

Wang Chuchu C   Zhao Chunyu C   Li Dan D   Tian Zhiqi Z   Lai Ying Y   Diao Jiajie J   Liu Cong C  

Frontiers in molecular neuroscience 20160620


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 activiti  ...[more]

Similar Datasets

| S-EPMC7038196 | biostudies-literature
| S-EPMC3605821 | biostudies-other
| S-EPMC7116528 | biostudies-literature
| S-EPMC5209871 | biostudies-literature
| S-EPMC3715894 | biostudies-other
| S-EPMC6989544 | biostudies-literature
| S-EPMC4932447 | biostudies-literature
| PRJNA666729 | ENA
| PRJNA575845 | ENA
| S-EPMC7155127 | biostudies-literature