Proceedings of the National Academy of Sciences · 1999 · 260 citations · 27 references
Life SciencesCell BiologyMolecular BiologyMembrane BiochemistryMembrane BiophysicsStructural BiologyBiological MembranesMacromolecular AssemblyMembrane FusionMembrane Protein TopologySnare-mediated FusionVesicle FusionHelical ConformationLipid VesiclesMembrane Snare ComplexesSnare Complex AssemblySnare ProteinsSnare-mediated Membrane FusionSnare-mediated Vesicle FusionVesicle Fusion Machinery
A protease-resistant core domain of the neuronal SNARE complex consists of an alpha-helical bundle similar to the proposed fusogenic core of viral fusion proteins [Skehel, J. J. & Wiley, D. C. (1998) Cell 95, 871-874]. We find that the isolated core of a SNARE complex efficiently fuses artificial bilayers and does so faster than full length SNAREs. Unexpectedly, a dramatic increase in speed results from removal of the N-terminal domain of the t-SNARE syntaxin, which does not affect the rate of assembly of v-t SNARES. In the absence of this negative regulatory domain, the half-time for fusion of an entire population of lipid vesicles by isolated SNARE cores ( approximately 10 min) is compatible with the kinetics of fusion in many cell types.
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SNAP receptors implicated in vesicle targeting and fusion
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Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 Å resolution
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