ArticleProceedings of the National Academy of Sciences of the United States of America2009
A scissors mechanism for stimulation of SNARE-mediated lipid mixing by cholesterol.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
55 citing papers in PubMed, 113 citations in OpenAlex.
- Turbocharging synaptic transmission: 12 SNAREpins are required for rapid release of reconstituted synaptic vesicles.Science advances · 2026Article
- Synaptobrevin2 monomers and dimers differentially engage to regulate the functional trans-SNARE assembly.Life science alliance · 2024Article
- Synaptophysin chaperones the assembly of 12 SNAREpins under each ready-release vesicle.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Structural insights into perilipin 3 membrane association in response to diacylglycerol accumulation.Nature communications · 2023Article
- MeCP2 Is an Epigenetic Factor That Links DNA Methylation with Brain Metabolism.International journal of molecular sciences · 2023Review
- Article
- Drunken lipid membranes, not drunken SNARE proteins, promote fusion in a model of neurotransmitter release.Frontiers in molecular neuroscience · 2022Article
- Phosphatidylinositol and phosphatidylinositol-3-phosphate activate HOPS to catalyze SNARE assembly, allowing small headgroup lipids to support the terminal steps of membrane fusion.Molecular biology of the cell · 2021Article
- Cholesterol stabilizes recombinant exocytic fusion pores by altering membrane bending rigidity.Biophysical journal · 2021Article
- Synaptic Function and Dysfunction in Lysosomal Storage Diseases.Frontiers in cellular neuroscience · 2021Article
- Hybrid methods for combined experimental and computational determination of protein structure.The Journal of chemical physics · 2020Review
- Article
- Lipid rafts and pathogens: the art of deception and exploitation.Journal of lipid research · 2020Review
- The Effects of Regulatory Lipids on Intracellular Membrane Fusion Mediated by Dynamin-Like GTPases.Frontiers in cell and developmental biology · 2020Review
- ApoE4-Induced Cholesterol Dysregulation and Its Brain Cell Type-Specific Implications in the Pathogenesis of Alzheimer's Disease.Molecules and cells · 2019Review
- EPR Lineshape Analysis to Investigate the SNARE Folding Intermediates.Methods in molecular biology (Clifton, N.J.) · 2019Review
- Toward a unified picture of the exocytotic fusion pore.FEBS letters · 2018Review
- v-SNARE function in chromaffin cells.Pflugers Archiv : European journal of physiology · 2018Review
- Membrane Fusion Stalks and Lipid Rafts: A Love-Hate Relationship.Biophysical journal · 2017Article
- A Central Small Amino Acid in the VAMP2 Transmembrane Domain Regulates the Fusion Pore in Exocytosis.Scientific reports · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
Abstract
Neurotransmitter release at the synapse requires membrane fusion. The SNARE complex, composed of the plasma membrane t-SNAREs syntaxin 1A and SNAP-25 and the vesicle v-SNARE synaptobrevin, mediates the fusion of 2 membranes. Synaptic vesicles contain unusually high cholesterol, but the exact role of cholesterol in fusion is not known. In this study, cholesterol was found to stimulate SNARE-mediated lipid mixing of proteoliposomes by a factor of 5 at a physiological concentration. Surprisingly, however, the stimulatory effect was more pronounced when cholesterol was on the v-SNARE side than when it was on the t-SNARE side. Site-directed spin labeling and both continuous wave (CW) and pulsed EPR revealed that cholesterol induces a conformational change of the v-SNARE transmembrane domain (TMD) from an open scissors-like dimer to a parallel dimer. When the TMD was forced to form a parallel dimer by the disulfide bond, the rate was stimulated 2.3-fold even without cholesterol, supporting the relevance of the open-to-closed conformational change to the fusion activity. The open scissors-like conformation may be unfavorable for fusion and cholesterol may relieve this inhibitory factor.
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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.