Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 15, Issue 7, Pages 665-674Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.1450
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Funding
- NINDS NIH HHS [R01 NS051262, NS37200, R01 NS037200, R01 NS040944, R01 NS051262-04, NS40944, R01 NS040944-08, R01 NS050655, R01 NS037200-08, NS050655, NS051262, R01 NS050655-03] Funding Source: Medline
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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.
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