Abstract
α-synuclein (α-Syn) is a presynaptic enriched protein involved in the pathogenesis of Parkinson’s disease. However, the physiological roles of α-Syn remain poorly understood. Recent studies have indicated a critical role of α-Syn in the sensing and generation of membrane curvature during vesicular exocytosis and endocytosis. It has been known to modulate the assembly of SNARE complex during exocytosis including vesicle docking, priming and fusion steps. Growing evidence suggests that α-Syn also plays critical roles in the endocytosis of synaptic vesicles. It also modulates the availability of releasable vesicles by promoting synaptic vesicles clustering. Here, we provide an overview of recent progresses in understanding the function of α-Syn in the regulation of exocytosis, endocytosis, and vesicle recycling under physiological and pathological conditions.
Highlights
Specialty section: This article was submitted to Neurodegeneration, a section of the journal Frontiers in Neuroscience
Α-synuclein is abundant in presynapse and interacts with synaptic vesicles (SVs) to modulate vesicle recycling physiologically (Maroteaux et al, 1988; Jensen et al, 1998). α-Syn plays critical roles in PD pathogenesis
Among the PD-linked mutations, A53T is located at the dimer interface of the fibril and E46K is related to the stabilization of the protofilament
Summary
Specialty section: This article was submitted to Neurodegeneration, a section of the journal Frontiers in Neuroscience. Recent studies have indicated a critical role of α-Syn in the sensing and generation of membrane curvature during vesicular exocytosis and endocytosis.
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