Abstract
Most communication between neurons is achieved at synapses by the process of neurotransmitter release. Neurotransmitter release is initiated by depolarization of a neuron, which in turn activates voltage-gated Ca2+ channels. The resulting Ca2+ influx then triggers the fusion of the synaptic vesicles with the plasma membrane. Synaptic vesicle fusion is mediated by a core fusion machinery SNARE complex, a small regulatory factor complexin (Cpx), and Ca2+ sensor synaptotagmin (Syt). However, it was unknown how they cooperate to trigger synaptic vesicle fusion. Combining X-ray crystallography and electrophysiological recording techniques, we determined two atomic resolution crystal structures of the synaptic vesicle fusion machinery at different states, revealing a large, specific, Ca2+-independent interface which is essential for synchronous neurotransmitter release in mouse neuronal synapses. We propose a working model and further reveal the molecular mechanism of synchronous neurotransmitter release.
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