Thomas Binz

TL;DR: It is demonstrated that BoNT/A acts as a zinc-dependent protease that selectively cleaves SNAP-25, a second component of the putative fusion complex mediating synaptic vesicle exocytosis is targeted by a clostridial neurotoxin.

TL;DR: The data suggest that synaptobrevin, syntaxin and SNAP‐25 associate into a unique stable complex that functions in synaptic vesicle exocytosis, suggesting that membrane fusion involves intermolecular interactions via coiled‐coil structures.

TL;DR: It is concluded that HPC‐1/syntaxin, a membrane protein present in axonal and synaptic membranes, is involved in exocytotic membrane fusion.

TL;DR: The results suggest that constitutive and regulated vesicular pathways use homologous proteins for membrane trafficking, probably for membrane fusion at the plasma membrane, indicating a greater mechanistic and evolutionary similarity between these pathways than previously thought.

TL;DR: BoNT/E, like BoNT/A, cleaves SNAP-25, as generated by in vitro translation or by expression in Escherichia coli, and further support the view that clostridial neurotoxins have evolved from an ancestral protease recognizing the exocytotic fusion machinery of synaptic vesicles whereby individual toxins target different members of the membrane fusion complex.