Structure, dynamics, and mutation of a gamete fusion protein and comparisons to viral homologues suggest that after trimerization the domain bearing the membrane-inserting fusion loops can pivot with respect to the trimer 3-fold axis.

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

Molecular, genetic, and functional analysis is used to show that the olfactory Na+/Ca2+, K+ exchanger NCKX4 is expressed in cone photoreceptors and is critical for the wide operating range and high temporal resolution of cone-mediated vision.

Structural flexibility of the synaptobrevin-2 transmembrane domain promotes membrane fusion.

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

Mitochondrial fusion enables a metabolic transition during spermatogenesis.

Induction of the fission of mitochondria-populating sensory axons is shown to be a novel biological action of neurotrophins.

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.

A combination of advanced optical imaging and cryogenic electron microscopy has been used to explore membrane fusion in a synthetic system and provide new insights into neurotransmitter release.

The SNAP-25 linker acts as a functional component of SNARE complexes, initially facilitating SNARE interactions and later promoting fusion triggering and pore evolution by local membrane contacts.