SNAP-mediated protein–protein interactions essential for neurotransmitter release

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Abstract
THE constitutive fusion of transport vesicles with intracellular membranes requires soluble proteins called SNAPs1. Certain pre-synaptic proteins2–1 implicated in synaptic vesicle exocytosis5 also bind SNAPs, suggesting that SNAPs participate in the calcium-regulated membrane fusion events mediating neurotransmitter release6,7. Here we show that injection of recombinant SNAPs into the giant synapse of squid enhances transmitter release. Conversely, injection of peptides designed to mimic the sites at which SNAP interacts with its binding partners inhibits transmitter release downstream of synaptic vesicle docking. A SNAP-dependent protein complex must therefore mediate transmitter release, showing that transmitter release shares a common molecular mechanism with constitutive membrane fusion.