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Significance The accumulation of nonfunctional α-synuclein (α-synFL ) oligomers is the hallmark of Parkinson’s disease (PD), affecting millions of people worldwide. Although α-synFL has a central role in PD, its cellular function is unclear until now. Understanding the normal function of α-synFL is critical to envisage the molecular basis of abnormal cellular secretion under disease conditions. Previous studies indicated that it can regulate various steps of membrane fusion. Fusion pores are the crucial kinetic intermediates during membrane fusion, through which vesicular secretion occurs from different cell types. Here, we describe a function of α-synFL in regulating the microsecond fusion pore transitions. This study offers an insight into how abnormal secretion occurs under pathological conditions in which nonfunctional α-synFL accumulates.

α-Synuclein kinetically regulates the nascent fusion pore dynamics