The precise position of UNC-13 at the active zone near a synapse depends on the N-terminus of the protein, and the C₂A domain in particular, and is essential for accelerating neurotransmitter release.

Sec1/Munc18 (SM) proteins shield SNARE complexes from NSF/Sec18-mediated disassembly through cooperative binding interactions with SNARE complexes and the universal co-chaperone α-SNAP/Sec17.

Rigorous assays of membrane fusion show that a distinct tethering step is required for lumenal compartment mixing in a manner that extends beyond simply increasing the amount of total trans-SNARE complex.

An unconventional endosomal tether in Drosophila melanogaster only has four of the six subunits found in the yeast complex.

SNARE proteins are delivered as complexes already from the endoplasmic reticulum along the secretory pathway to the cell division plane to mediate the formation of the partitioning membrane by vesicle fusion.

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.

Sec17 (αSNAP) and Sec18 (NSF) are shown to act twice, to promote fusion per se and to recycle SNAREs after fusion.

Sec1/Munc18-family proteins chaperone SNARE assembly via a common templating mechanism.

The tethering complex HOPS employs affinity for each of the 4 SNAREs to catalyze assembly of 3-SNARE intermediates, supporting an immediate burst of membrane fusion triggered by the 4th SNARE.