Fig. 1

A Schematic of the domain structures, genetic mutations, and posttranscriptional modifications of α-syn related to Parkinson’s disease (PD). The α-synuclein (α-syn) protein comprises three domains: the N-terminal amphipathic region, the nonamyloidogenic component (NAC) domain, and the C-terminal acidic domain. All identified disease-linked mutations are in the N-terminal domain. Mutation sites related to diseases are shown in red; these sites can be posttranslationally modified. B Transition of the monomeric form of α-syn to a pathological aggregate. Native forms of α-syn exist physiologically and can be folded into oligomers. Monomers form fibrils through a nucleated polymerization mechanism, and an equilibrium between fibrils and monomeric α-syn is maintained. The aggregation of amyloid fibrils results in the formation of intracellular deposits referred to as Lewy bodies (LBs)