The docking of synaptic vesicles on the presynaptic membrane induced by α-synuclein is modulated by lipid composition.

ABSTRACT: α-Synuclein (αS) is a presynaptic disordered protein whose aberrant aggregation is associated with Parkinson's disease. The functional role of αS is still debated, although it has been involved in the regulation of neurotransmitter release via the interaction with synaptic vesicles (SVs). We report here a detailed characterisation of the conformational properties of αS bound to the inner and outer leaflets of the presynaptic plasma membrane (PM), using small unilamellar vesicles. Our results suggest that αS preferentially binds the inner PM leaflet. On the basis of these studies we characterise in vitro a mechanism by which αS stabilises, in a concentration-dependent manner, the docking of SVs on the PM by establishing a dynamic link between the two membranes. The study then provides evide

SUBMITTER: Man WK 

PROVIDER: S-EPMC7876145 | biostudies-literature | 2021 Feb

REPOSITORIES: biostudies-literature