A new insight into the role of syntaxin1's juxtamembrane region in controlling palmitoylation and spontaneous neurotransmitter release.

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

Genetics and genomics approaches reveal a conserved post-transcriptional regulatory mechanism that promotes adult axon regeneration from worm to mammals.

A new native prion protein aggregation assay shows that syntaxin-6, a risk factor for sporadic Creutzfeldt–Jakob disease, delays prion protein fibril formation and prolongs the presence of toxic aggregation intermediates.

Genetic and electrophysiological experiments define how homeostatic signaling stabilizes both the gain and short-term dynamic properties of neurotransmitter release, ensuring that synaptic information transfer remains robust to external perturbation.

Biophysical and functional data strongly support the notion that Munc18-1 acts as a template to assemble the neuronal SNARE complex, and that inhibition of this activity underlies diverse forms of regulation of neurotransmitter release.

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.

SNARE–SNARE interactions that have previously only been proposed to participate in membrane fusion on the nanoscale also serve to organize SNARE domains on the mesoscale.

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

A mutant rescue approach in STX1-null autaptic neurons provides definitive answers and opens up new questions into a controversial matter of syntaxin-1's binding to Munc18-1 through its N-peptide and its function in neurotransmission.