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Review
. 2021 Mar 4:15:633727.
doi: 10.3389/fncel.2021.633727. eCollection 2021.

The Membrane Interaction of Alpha-Synuclein

Cencen Liu  1 , Yunfei Zhao  1 , Huan Xi  1 , Jie Jiang  1 , Yang Yu  2 , Wei Dong  1   3   4
Affiliations
Review

The Membrane Interaction of Alpha-Synuclein

Cencen Liu et al. Front Cell Neurosci. .

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.

Keywords: Parkinson's disease; SNAREs; alpha-synuclein; membrane; synaptic transmission.

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Conflict of interest statement

The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.

Figures

Figure 1
Figure 1
Schematic diagram of α-Syn in SNARE (a complex composed of syntaxin-1A, VAMP2 and SNAP-25)-mediated membrane interaction. α-Syn's N-terminus forms two helices to interact with the plasma membrane, while α-Syn interacts with VAMP2 at the C-terminus.
See this image and copyright information in PMC

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