Review abstract
Focus on Membrane Fusion
- Focus issue:
- Julember 2008 Volume 15, No 7
Nature Structural & Molecular Biology 15, 665 - 674 (2008)
Published online: 3 July 2008 | doi:10.1038/nsmb.1450
Synaptic vesicle fusion
Josep Rizo1 & Christian Rosenmund2
Abstract
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.
- Departments of Biochemistry and Pharmacology, University of Texas Southwestern Medical Center, 6000 Harry Hines Boulevard, Dallas, Texas 75390, USA.
- Departments of Neuroscience and Molecular and Human Genetics, Baylor College of Medicine, One Baylor Plaza, Houston, Texas 77030, USA.
Correspondence to: Josep Rizo1 e-mail: jose@arnie.swmed.edu
Correspondence to: Christian Rosenmund2 e-mail: rosenmun@bcm.tmc.edu
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