Publication | Closed Access
N- to C-Terminal SNARE Complex Assembly Promotes Rapid Membrane Fusion
396
Citations
19
References
2006
Year
Molecular BiologyExtracellular MicrovesiclesCytoskeletonLiposome FusionCellular PhysiologyMembrane FusionMembrane TransportSynaptic VesiclesEndocytic PathwaySecretory PathwayCell SignalingMulti-protein AssemblyBiophysicsCell TraffickingWhereas ExocytosisMembrane BiologyMembrane SystemCell BiologyMembrane BiophysicsSignal TransductionNatural SciencesIntracellular TraffickingCellular BiochemistrySystems BiologyMedicine
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.
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