The Membrane Interaction of Alpha-Synuclein.

Abstract

A presynaptic protein closely related to Parkinson's disease (PD), α-synuclein (α-Syn), has been studied extensively regarding its pathogenic mechanisms. As a physiological protein in presynapses, however, α-Syn's physiological function remains unclear. Its location in nerve terminals and effects on membrane fusion also imply its functional role in synaptic transmission, including its possible interaction with high-curvature membranes via its N-terminus and amorphous C-terminus. PD-related mutants that disrupt the membrane interaction (e.g., A30P and G51D) additionally suggest a relationship between α-Syn's pathogenic mechanisms and physiological roles through the membrane binding. Here, we summarize recent research on how α-Syn and its variants interact with membranes and influence synaptic transmission. We list several membrane-related connections between the protein's physiological function and the pathological mechanisms that stand to expand current understandings of α-Syn.

• Authors: Cencen Liu, Yunfei Zhao, Huan Xi, Jie Jiang, Yang Yu, Wei Dong
• Journal: Frontiers in cellular neuroscience (Front Cell Neurosci) Vol. 15 Pg. 633727 ( 2021) ISSN: 1662-5102 [Print] Switzerland
• PMID: 33746714 (Publication Type: Journal Article, Review)
• Copyright: Copyright © 2021 Liu, Zhao, Xi, Jiang, Yu and Dong.