Determinants of liposome fusion mediated by synaptic SNARE proteins.
作者： C. G. Schuette , K. Hatsuzawa , M. Margittai , A. Stein , D. Riedel
关键词: Vesicle fusion 、 Exocytosis 、 Vesicle 、 Syntaxin 1 、 Lipid bilayer fusion 、 Munc-18 、 Cell biology 、 STX1A 、 Synaptobrevin 、 Biology
摘要: Synaptic exocytosis requires the soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) proteins syntaxin 1, SNAP-25, and synaptobrevin (VAMP). Assembly of SNAREs into a stable core complex is supposed to catalyze membrane fusion, proteoliposomes reconstituted with synaptic SNARE spontaneously fuse each other. We now show that liposome fusion mediated by inhibited botulinum neurotoxin E (BoNT/E) but can be rescued supplementing C-terminal portion SNAP-25. Furthermore, prevented SNAP-25-specific antibody known block in chromaffin cells, it competed for fragments R-SNAREs 2, endobrevin/VAMP-8, tomosyn. No accumulation clustered vesicles observed during reaction. Rapid artificial clustering SNARE-containing enhances rate at low not saturating concentrations. conclude dominated intrinsic properties rather than preceding docking step.
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