The crystal structure of a large C-terminal fragment of Munc13-1 provides a key framework to understand how Munc13-1 mediates neurotransmitter release and presynaptic plasticity.

Synaptic vesicles undergo reversible tethering at the plasma membrane which is activity- and myosin V- dependent.

Cryo-electron tomography, reconstitution, and electrophysiological data show that a fundamental function of Munc13-1 is to bridge synaptic vesicles to the presynaptic plasma membrane.

Challenging a widespread model, biophysical and electrophysiological experiments suggest a new mechanism whereby complexins inhibit neurotransmitter release through electrostatic repulsion between their accessory helix and the membranes.

A combination of advanced optical imaging and cryogenic electron microscopy has been used to explore membrane fusion in a synthetic system and provide new insights into neurotransmitter release.

Biophysical and functional data strongly support the notion that Munc18-1 acts as a template to assemble the neuronal SNARE complex, and that inhibition of this activity underlies diverse forms of regulation of neurotransmitter release.

Neurons of the cholinergic system, which release the excitatory neurotransmitter acetycholine throughout the cortex, also release the inhibitory transmitter GABA, with potential implications for cognitive function.

Long and short variants of a protein called UNC-13, assisted by another called Tomosyn, regulate the timing of synaptic vesicle release in C. elegans.

Structural flexibility of the synaptobrevin-2 transmembrane domain promotes membrane fusion.

Complexin can have two conformations when bound to a ternary SNARE complex, one of which induces a conformational change of the SNARE complex at the C-terminus.