Synaptic vesicle fusion.
The core of the neurotransmitter release machinery is formed by SNARE complexes, which bring the vesicle and plasma membranes together and are key for fusion, and by Munc18-1, which controls SNARE-complex formation and may also have a direct role in fusion. In addition, SNARE complex assembly is likely orchestrated by Munc13s and RIMs, active-zone proteins that function in vesicle priming and diverse forms of presynaptic plasticity. Synaptotagmin-1 mediates triggering of release by Ca2+, probably through interactions with SNAREs and both membranes, as well as through a tight interplay with complexins. Elucidation of the release mechanism will require a full understanding of the network of interactions among all these proteins and the membranes.
Rizo
Josep
J
Department of Biochemistry, University of Texas Southwestern Medical Center, 6000 Harry Hines Boulevard, Dallas, Texas 75390, USA. jose@arnie.swmed.edu
Rosenmund
Christian
C
D000818:Animals; D008561:Membrane Fusion / Q000502:physiology*; D051938:Munc18 Proteins / Q000737:chemistry / Q000378:metabolism; D009419:Nerve Tissue Proteins / Q000737:chemistry / Q000378:metabolism; D050600:SNARE Proteins / Q000737:chemistry / Q000378:metabolism; D013572:Synaptic Vesicles / Q000378:metabolism*; D050863:Synaptotagmin I / Q000737:chemistry / Q000378:metabolism
D051938:Munc18 Proteins; D009419:Nerve Tissue Proteins; D050600:SNARE Proteins; D050863:Synaptotagmin I