α-Synuclein can inhibit SNARE-mediated vesicle fusion through direct interactions with lipid bilayers

Biochemistry. 2013 Apr 9;52(14):2385-7. doi: 10.1021/bi4002369. Epub 2013 Mar 27.

Abstract

The native function of α-synuclein is thought to involve regulation of synaptic vesicle trafficking. Recent work has also implicated a role in neurotransmission, possibly through interactions with the proteins involved in synaptic vesicle fusion. Here, we demonstrate that α-synuclein inhibits SNARE-mediated vesicle fusion through binding the membrane, without a direct interaction between α-synuclein and any of the SNARE proteins. This work supports a model in which α-synuclein plays a role in the regulation of vesicle fusion by modulating properties of the lipid bilayer.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Humans
  • Lipid Bilayers / metabolism*
  • Membrane Fusion*
  • Recombinant Proteins / metabolism
  • SNARE Proteins / metabolism*
  • alpha-Synuclein / metabolism*

Substances

  • Lipid Bilayers
  • Recombinant Proteins
  • SNARE Proteins
  • alpha-Synuclein