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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.

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

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.

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.

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.