Temperature-Sensitive Paralytic Mutations Demonstrate that Synaptic Exocytosis Requires SNARE Complex Assembly and Disassembly
Copyright policy )Temperature-Sensitive Paralytic Mutations Demonstrate that Synaptic Exocytosis Requires SNARE Complex Assembly and Disassembly
The neuronal SNARE complex is formed via the interaction of synaptobrevin with syntaxin and SNAP-25. Purified SNARE proteins assemble spontaneously, while disassembly requires the ATPase NSF. Cycles of assembly and disassembly have been proposed to drive lipid bilayer fusion. However, this hypothesis remains to be tested in vivo. We have isolated a Drosophila temperature-sensitive paralytic mutation in syntaxin that rapidly blocks synaptic transmission at nonpermissive temperatures. This paralytic mutation specifically and selectively decreases binding to synaptobrevin and abolishes assembly of the 7S SNARE complex. Temperature-sensitive paralytic mutations in NSF (comatose) also block synaptic transmission, but over a much slower time course and with the accumulation of syntaxin and SNARE complexes on synaptic vesicles. These results provide in vivo evidence that cycles of assembly and disassembly of SNARE complexes drive membrane trafficking at synapses.
- University of Wisconsin–Madison United States
- University of Wisconsin–Oshkosh United States
Neurotransmitter Agents, Sequence Homology, Amino Acid, Qa-SNARE Proteins, Neuroscience(all), Molecular Sequence Data, Temperature, Vesicular Transport Proteins, Membrane Proteins, Nerve Tissue Proteins, Exocytosis, Recombinant Proteins, Culture Techniques, Mutation, Synapses, Animals, Paralysis, Drosophila, Amino Acid Sequence, Synaptic Vesicles, SNARE Proteins
Neurotransmitter Agents, Sequence Homology, Amino Acid, Qa-SNARE Proteins, Neuroscience(all), Molecular Sequence Data, Temperature, Vesicular Transport Proteins, Membrane Proteins, Nerve Tissue Proteins, Exocytosis, Recombinant Proteins, Culture Techniques, Mutation, Synapses, Animals, Paralysis, Drosophila, Amino Acid Sequence, Synaptic Vesicles, SNARE Proteins
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