期刊
EMBO JOURNAL
卷 31, 期 9, 页码 2156-2168出版社
WILEY
DOI: 10.1038/emboj.2012.72
关键词
exocytosis; Munc18-1; SM proteins; SNARE complex; Syntaxin1a
资金
- EU [019055, HEALTH-F2-2009-241498, HEALTH-F2-2009-242167]
- Netherlands Organization for Scientific Research, NWO [Pionier/VICI 900-01-001, ZonMW 903-42-095, VENI 916-36043]
- NeuroBsik Mouse Phenomics Consortium [BSIK03053]
Synaptic transmission depends critically on the Sec1p/Munc18 protein Munc18-1, but it is unclear whether Munc18-1 primarily operates as a integral part of the fusion machinery or has a more upstream role in fusion complex assembly. Here, we show that point mutations in Munc18-1 that interfere with binding to the free Syntaxin1a N-terminus and strongly impair binding to assembled SNARE complexes all support normal docking, priming and fusion of synaptic vesicles, and normal synaptic plasticity in munc18-1 null mutant neurons. These data support a prevailing role of Munc18-1 before/during SNARE-complex assembly, while its continued association to assembled SNARE complexes is dispensable for synaptic transmission. The EMBO Journal (2012) 31, 2156-2168. doi:10.1038/emboj.2012.72; Published online 23 March 2012
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