Sec18(NSF) and Sec17(αSNAP) provide a parallel pathway to fusion that is independent of energy from SNARE zippering.

The first quantitative live-cell microscopy this work shows depicting the order of events preceding secretion in budding yeast.

Unconventional secretion of a plasma membrane purine transporter via Golgi-bypass is established at an early ER-associated secretory compartment revealing that specific cargoes define alternative trafficking routes.

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.

Phosphorylation of a core trafficking component, the COPII coat subunit Sec24, regulates cross-talk between the secretory and autophagy machinery during starvation.

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

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.

The coordinate activity of Sec17/SNAP and Sec18/NSF for membrane fusion is not limited to systems with homotypic fusion and vacuole protein sorting (HOPS), the lysosomal/vacuolar tethering, and SNARE assembly complex.

A structure of the complete, membrane bound, COPII coat solved by sub-tomogram averaging reveals the arrangement of all protein subunits on the membrane and suggests a mechanism for coating heterogeneously-shaped carriers.

A new class of fungal hemoproteins is described that emphasizes the versatility of the Sec14-fold for translating binding of chemically distinct ligands to control of diverse sets of cellular activities.