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SNAREpins: minimal machinery for membrane fusion. Munc13 mediates the transition from the closed syntaxin-Munc18 complex to the SNARE complex. Membrane fusion: grappling with SNARE and SM proteins. A complexin/synaptotagmin 1 switch controls fast synaptic vesicle exocytosis. Fusion pores and fusion machines in Ca 2+-triggered exocytosis. Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 Å resolution. SNAP receptors implicated in vesicle targeting and fusion.
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Techniques and concepts in exocytosis: focus on mast cells. Mechanisms underlying phasic and sustained secretion in chromaffin cells from mouse adrenal slices. Peptide secretion: what do we know? FASEB J. Spontaneous and evoked activity of motor nerve endings in calcium Ringer. Our system is unique in that it monitors both content and lipid mixing and starts from a metastable state of interacting vesicle pairs before Ca 2+ injection. Other factors such as complexin can be easily added. Upon Ca 2+ injection into the sample chamber, our system therefore differentiates between hemifusion and complete fusion of interacting vesicle pairs and determines the temporal sequence of these events on a sub-100-millisecond time scale. The donor vesicles also contain two spectrally distinct fluorophores that allow simultaneous monitoring of temporal changes of the content and membrane. Donor vesicles are mixed with the tethered acceptor vesicles and incubated for several minutes at a zero-Ca 2+ concentration, resulting in a collection of single interacting vesicle pairs. Acceptor vesicles contain reconstituted syntaxin and synaptosomal-associated protein 25 (SNAP-25), and they are tethered to a PEG-coated glass surface. Donor vesicles contain reconstituted synaptobrevin and synaptotagmin-1. This protocol describes a single vesicle-vesicle microscopy system to study Ca 2+-triggered vesicle fusion.