title: α-Synuclein can inhibit SNARE-mediated vesicle fusion through direct interactions with lipid bilayers.
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.
authors.affiliation: Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06511, USA.
authors.forename: David C
authors.initials: DC
authors.lastname: DeWitt
authors.forename: Elizabeth
authors.initials: E
authors.lastname: Rhoades
mesh_terms: D000818:Animals; D006801:Humans; D008051:Lipid Bilayers / Q000378:metabolism*; D008561:Membrane Fusion; D011994:Recombinant Proteins / Q000378:metabolism; D050600:SNARE Proteins / Q000378:metabolism*; D051844:alpha-Synuclein / Q000378:metabolism*
chemical_list: D008051:Lipid Bilayers; D011994:Recombinant Proteins; D050600:SNARE Proteins; D051844:alpha-Synuclein