Molecular Mechanisms of Synaptic Vesicle Priming by Munc13 and Munc18
2017 | journal article
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Cite this publication
Molecular Mechanisms of Synaptic Vesicle Priming by Munc13 and Munc18
Lai, Y.; Choi, U. B.; Leitz, J.; Rhee, H. J.; Lee, C.; Altas, B. & Zhao, M. et al. (2017)
Neuron, 95(3) pp. 591-607.e10. DOI: https://doi.org/10.1016/j.neuron.2017.07.004
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Details
- Authors
- Lai, Ying; Choi, Ucheor B.; Leitz, Jeremy; Rhee, Hong Jun; Lee, Choongku; Altas, Bekir; Zhao, Minglei; Pfuetzner, Richard A.; Wang, Austin L.; Brose, Nils ; Rhee, JeongSeop ; Brunger, Axel T.
- Abstract
- Munc13 catalyzes the transit of syntaxin from a closed complex with Munc18 into the ternary SNARE complex. Here we report a new function of Munc13, independent of Munc18: it promotes the proper syntaxin/synaptobrevin subconfiguration during assembly of the ternary SNARE complex. In cooperation with Munc18, Munc13 additionally ensures the proper syntaxin/SNAP-25 subconfiguration. In a reconstituted fusion assay with SNAREs, complexin, and synaptotagmin, inclusion of both Munc13 and Munc18 quadruples the Ca2+-triggered amplitude and achieves Ca2+ sensitivity at near-physiological concentrations. In Munc13-1/2 double-knockout neurons, expression of a constitutively open mutant of syntaxin could only minimally restore neurotransmitter release relative to Munc13-1 rescue. Together, the physiological functions of Munc13 may be related to regulation of proper SNARE complex assembly.
- Issue Date
- 2017
- Journal
- Neuron
- ISSN
- 0896-6273; 0896-6273
- Language
- English