The Membrane Interaction of Alpha-Synuclein

A presynaptic protein closely related to Parkinson's disease (PD), alpha-synuclein (alpha-Syn), has been studied extensively regarding its pathogenic mechanisms. As a physiological protein in presynapses, however, alpha-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 alpha-Syn's pathogenic mechanisms and physiological roles through the membrane binding. Here, we summarize recent research on how alpha-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 alpha-Syn.

Automated summary

The presynaptic protein alpha-synuclein (alpha-Syn), closely related to Parkinson's disease, has been extensively studied for its pathogenic mechanisms. Its interaction with membranes and influence on synaptic transmission may provide insights into both its pathology and physiological functions. Research on alpha-Syn and its variants interacting with membranes stands to expand current understandings of the protein.