ArticleThe Journal of biological chemistry2015
Munc18a does not alter fusion rates mediated by neuronal SNAREs, synaptotagmin, and complexin.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 19 citations in OpenAlex.
- The function of VAMP2 in mediating membrane fusion: An overview.Frontiers in molecular neuroscience · 2022Review
- Article
- New Insights Into Interactions of Presynaptic Calcium Channel Subtypes and SNARE Proteins in Neurotransmitter Release.Frontiers in molecular neuroscience · 2018Article
- Munc18a clusters SNARE-bearing liposomes prior toThe Biochemical journal · 2017Article
- An activated Q-SNARE/SM protein complex as a possible intermediate in SNARE assembly.The EMBO journal · 2017Article
- SM protein Munc18-2 facilitates transition of Syntaxin 11-mediated lipid mixing to complete fusion for T-lymphocyte cytotoxicity.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Membrane Fusion Involved in Neurotransmission: Glimpse from Electron Microscope and Molecular Simulation.Frontiers in molecular neuroscience · 2017Review
- Article
- Chaperoning SNARE assembly and disassembly.Nature reviews. Molecular cell biology · 2016Review
- Extension of Helix 12 in Munc18-1 Induces Vesicle Priming.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2016Article
- Article
- Synaptotagmin-1 is an antagonist for Munc18-1 in SNARE zippering.The Journal of biological chemistry · 2015Article
- Curcumin inhibits the proliferation and invasion of human osteosarcoma cell line MG-63 by regulating miR-138.International journal of clinical and experimental pathology · 2015Article
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Authors and funding
13 authors at 2 institutions in 1 country.
Funding
Abstract
Sec1/Munc18 (SM) proteins are essential for membrane trafficking, but their molecular mechanism remains unclear. Using a single vesicle-vesicle content-mixing assay with reconstituted neuronal SNAREs, synaptotagmin-1, and complexin-1, we show that the neuronal SM protein Munc18a/nSec1 has no effect on the intrinsic kinetics of both spontaneous fusion and Ca(2+)-triggered fusion between vesicles that mimic synaptic vesicles and the plasma membrane. However, wild type Munc18a reduced vesicle association ∼50% when the vesicles bearing the t-SNAREs syntaxin-1A and SNAP-25 were preincubated with Munc18 for 30 min. Single molecule experiments with labeled SNAP-25 indicate that the reduction of vesicle association is a consequence of sequestration of syntaxin-1A by Munc18a and subsequent release of SNAP-25 (i.e. Munc18a captures syntaxin-1A via its high affinity interaction). Moreover, a phosphorylation mimic mutant of Munc18a with reduced affinity to syntaxin-1A results in less reduction of vesicle association. In summary, Munc18a does not directly affect fusion, although it has an effect on the t-SNARE complex, depending on the presence of other factors and experimental conditions. Our results suggest that Munc18a primarily acts at the prefusion stage.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.