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- W2024251756 abstract "In neuroexocytosis, SNAREs and Munc18-1 may consist of the minimal membrane fusion machinery. Consistent with this notion, we observed, using single molecule fluorescence assays, that Munc18-1 stimulates SNARE zippering and SNARE-dependent lipid mixing in the absence of a major Ca2+ sensor synaptotagmin-1 (Syt1), providing the structural basis for the conserved function of Sec1/Munc18 proteins in exocytosis. However, when full-length Syt1 is present, no enhancement of SNARE zippering and no acceleration of Ca2+-triggered content mixing by Munc18-1 are observed. Thus, our results show that Syt1 acts as an antagonist for Munc18-1 in SNARE zippering and fusion pore opening. Although the Sec1/Munc18 family may serve as part of the fusion machinery in other exocytotic pathways, Munc18-1 may have evolved to play a different role, such as regulating syntaxin-1a in neuroexocytosis." @default.
- W2024251756 created "2016-06-24" @default.
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- W2024251756 date "2015-04-01" @default.
- W2024251756 modified "2023-09-29" @default.
- W2024251756 title "Synaptotagmin-1 Is an Antagonist for Munc18-1 in SNARE Zippering" @default.
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- W2024251756 doi "https://doi.org/10.1074/jbc.m114.631341" @default.
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