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

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 lysosome membrane is a new functional location for the ESCRTs in yeast.

A novel microscopy-based assay shows that dendritic cells encountering pathogenic stimuli form increased complexes of specific SNARE proteins, driving release of large amounts of inflammatory cytokines.

A molecular model of the assembled COPI coat, determined by cryo-electron tomography of an in vitro reconstituted budding reaction, reveals details of interactions mediating coat assembly and shows the binding site of ArfGAP2.

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.

Sec17 is shown to have divergent effects on pre-fusion SNARE complex activity, depending on the state of SNARE zippering and HOPS, an SM-tether complex, controls the outcome of Sec17-SNARE engagement.

COPI vesicle coat protein recognizes a ubiquitin sorting signal on an exocytic v-SNARE to mediate recycling.

Lipids with a propensity to form nonbilayer structures must be present for the last step of membrane fusion to take place.