Versatile Structures of α-Synuclein

Front Mol Neurosci. 2016 Jun 20:9:48. doi: 10.3389/fnmol.2016.00048. eCollection 2016.

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.

Keywords: Parkinson’s disease; amyloid; atomic structure; protein aggregation; vesicle trafficking; α-synuclein.

Publication types

  • Review