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N- to C-terminal SNARE complex assembly promotes rapid membrane fusion.
Assembly of the soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) syntaxin 1, SNAP-25, and synaptobrevin 2 is thought to be the driving force for the exocytosis of synaptic vesicles. However, whereas exocytosis is triggered at a millisecond time scale, the SNARE-mediated fusion of liposomes requires hours for completion, which challenges the idea of a key role for SNAREs in the final steps of exocytosis. We found that liposome fusion was dramatically accelerated when a stabilized syntaxin/SNAP-25 acceptor complex was used. Thus, SNAREs do have the capacity to execute fusion at a speed required for neuronal secretion, demonstrating that the maintenance of acceptor complexes is a critical step in biological fusion reactions.
Amino Acid Sequence, Animals, Binding Sites, Circular Dichroism, Dimerization, Exocytosis, Liposomes/chemistry, Membrane Fusion, Molecular Sequence Data, Peptide Fragments/chemistry, Peptide Fragments/metabolism, Protein Binding, Protein Folding, Protein Structure, Secondary, Qa-SNARE Proteins/chemistry, Qa-SNARE Proteins/metabolism, R-SNARE Proteins/chemistry, R-SNARE Proteins/metabolism, Rats, Synaptosomal-Associated Protein 25/chemistry, Synaptosomal-Associated Protein 25/metabolism
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