ArticlePloS one2008
Negative regulation of syntaxin4/SNAP-23/VAMP2-mediated membrane fusion by Munc18c in vitro.
Article in PloS one, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
What it found
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Who cites it
29 citing papers in PubMed, 45 citations in OpenAlex.
- The function of VAMP2 in mediating membrane fusion: An overview.Frontiers in molecular neuroscience · 2022Review
- Exocytosis in Astrocytes.Biomolecules · 2021Review
- Evidence for a conserved inhibitory binding mode between the membrane fusion assembly factors Munc18 and syntaxin in animals.The Journal of biological chemistry · 2017Article
- Suppression of VAMP2 Alters Morphology of the Tegument and Affects Glucose uptake, Development and Reproduction of Schistosoma japonicum.Scientific reports · 2017Article
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- Article
- Effects of immobilization and aerobic training on proteins related to intramuscular substrate storage and metabolism in young and older men.European journal of applied physiology · 2016Article
- Characterization of VAMP isoforms in 3T3-L1 adipocytes: implications for GLUT4 trafficking.Molecular biology of the cell · 2015Article
- Differential Effects of Munc18s on Multiple Degranulation-Relevant Trans-SNARE Complexes.PloS one · 2015Article
- Munc18c: a controversial regulator of peripheral insulin action.Trends in endocrinology and metabolism: TEM · 2014Review
- Review
- Insulin stimulates syntaxin4 SNARE complex assembly via a novel regulatory mechanism.Molecular and cellular biology · 2014Article
- Comparative studies of Munc18c and Munc18-1 reveal conserved and divergent mechanisms of Sec1/Munc18 proteins.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Specialized sorting of GLUT4 and its recruitment to the cell surface are independently regulated by distinct Rabs.Molecular biology of the cell · 2013Article
- Sorting of GLUT4 into its insulin-sensitive store requires the Sec1/Munc18 protein mVps45.Molecular biology of the cell · 2013Article
- Synip arrests soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE)-dependent membrane fusion as a selective target membrane SNARE-binding inhibitor.The Journal of biological chemistry · 2013Article
- Doc2b promotes GLUT4 exocytosis by activating the SNARE-mediated fusion reaction in a calcium- and membrane bending-dependent manner.Molecular biology of the cell · 2013Article
- Milligram quantities of homogeneous recombinant full-length mouse Munc18c from Escherichia coli cultures.PloS one · 2013Article
- Munc18-1 mutations that strongly impair SNARE-complex binding support normal synaptic transmission.The EMBO journal · 2012Article
- SNARE complex-mediated degranulation in mast cells.Journal of cellular and molecular medicine · 2012Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
backgroundTranslocation of the facilitative glucose transporter GLUT4 from an intracellular store to the plasma membrane is responsible for the increased rate of glucose transport into fat and muscle cells in response to insulin. This represents a specialised form of regulated membrane trafficking. Intracellular membrane traffic is subject to multiple levels of regulation by conserved families of proteins in all eukaryotic cells. Notably, all intracellular fusion events require SNARE proteins and Sec1p/Munc18 family members. Fusion of GLUT4-containing vesicles with the plasma membrane of insulin-sensitive cells involves the SM protein Munc18c, and is regulated by the formation of syntaxin 4/SNAP23/VAMP2 SNARE complexes. METHODOLOGY/PRINCIPAL
findingsHere we have used biochemical approaches to characterise the interaction(s) of Munc18c with its cognate SNARE proteins and to examine the role of Munc18c in regulating liposome fusion catalysed by syntaxin 4/SNAP23/VAMP2 SNARE complex formation. We demonstrate that Munc18c makes contacts with both t- and v-SNARE proteins of this complex, and directly inhibits bilayer fusion mediated by the syntaxin 4/SNAP23/VAMP2 SNARE complex. CONCLUSION/SIGNIFICANCE: Our reductionist approach has enabled us to ascertain a direct inhibitory role for Munc18c in regulating membrane fusion mediated by syntaxin 4/SNAP23/VAMP2 SNARE complex formation. It is important to note that two different SM proteins have recently been shown to stimulate liposome fusion mediated by their cognate SNARE complexes. Given the structural similarities between SM proteins, it seems unlikely that different members of this family perform opposing regulatory functions. Hence, our findings indicate that Munc18c requires a further level of regulation in order to stimulate SNARE-mediated membrane fusion.
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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 Socratic graph.