The Munc18-1 protein promotes formation of the t-SNARE complex and the half-zippered SNARE complex, two rate-limiting steps of SNARE assembly, to enhance membrane fusion.

The energy landscape of SNARE folding and assembly is optimized for efficient stage-wise membrane fusion.

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

Biophysical analyses indicate that Munc18-1, Munc13-1, synaptotagmin-1 and complexin-1 maintain assembled trans-SNARE complexes in the presence of NSF-alphaSNAP, suggesting that they form part of the primed state of synaptic vesicles.

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.

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.

A new binding mode between Rabphilin 3A and SNAP-25 enables efficient SNARE complex assembly via inducing a conformation change in SNAP-25 SNARE motif.

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.

Whereas in a paradigmatic structure an SM protein chaperone clamps its client SNARE shut, a second structure demonstrates that an SM protein can also hold its SNARE open to promote assembly.

NSF is part of a membrane trafficking quality control system that disassembles both properly formed and off-pathway SNARE complexes, and the disassembly activity may be regulated by complexin.