ArticleTraffic (Copenhagen, Denmark)2013
The lipid composition and physical properties of the yeast vacuole affect the hemifusion-fusion transition.
Article in Traffic (Copenhagen, Denmark), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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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.
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Who cites it
18 citing papers in PubMed, 37 citations in OpenAlex.
- Use of Bio-Layer Interferometry (BLI) to Measure Binding Affinities of SNAREs and Phosphoinositides.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Spectroscopic Methods for Detecting Conformational Changes During Sec18-Lipid Interactions.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Aspects of Biological Replication and Evolution Independent of the Central Dogma: Insights from Protein-Free Vesicular Transformations and Protein-Mediated Membrane Remodeling.The Journal of membrane biology · 2022Article
- Phosphatidylinositol 3,5-bisphosphate regulates CaTraffic (Copenhagen, Denmark) · 2020Article
- Copper blocks V-ATPase activity and SNARE complex formation to inhibit yeast vacuole fusion.Traffic (Copenhagen, Denmark) · 2019Article
- The Participation of Regulatory Lipids in Vacuole Homotypic Fusion.Trends in biochemical sciences · 2019Review
- Phosphatidic acid induces conformational changes in Sec18 protomers that prevent SNARE priming.The Journal of biological chemistry · 2019Article
- Phosphatidylinositol 3,5-bisphosphate regulates the transition between trans-SNARE complex formation and vacuole membrane fusion.Molecular biology of the cell · 2019Article
- Determination of Sec18-Lipid Interactions by Liposome-Binding Assay.Methods in molecular biology (Clifton, N.J.) · 2019Article
- Deleting the DAG kinase Dgk1 augments yeast vacuole fusion through increased Ypt7 activity and altered membrane fluidity.Traffic (Copenhagen, Denmark) · 2017Article
- How and why intralumenal membrane fragments form during vacuolar lysosome fusion.Molecular biology of the cell · 2017Article
- Steric hindrance of SNARE transmembrane domain organization impairs the hemifusion-to-fusion transition.EMBO reports · 2016Article
- Phosphatidic Acid Sequesters Sec18p from cis-SNARE Complexes to Inhibit Priming.Traffic (Copenhagen, Denmark) · 2016Article
- The Central Polybasic Region of the Soluble SNARE (Soluble N-Ethylmaleimide-sensitive Factor Attachment Protein Receptor) Vam7 Affects Binding to Phosphatidylinositol 3-Phosphate by the PX (Phox Homology) Domain.The Journal of biological chemistry · 2016Article
- Molecular Composition of Plant Vacuoles: Important but Less Understood Regulations and Roles of Tonoplast Lipids.Plants (Basel, Switzerland) · 2015Review
- A dynamin homolog promotes the transition from hemifusion to content mixing in intracellular membrane fusion.Traffic (Copenhagen, Denmark) · 2014Article
- The yeast ATP-binding cassette (ABC) transporter Ycf1p enhances the recruitment of the soluble SNARE Vam7p to vacuoles for efficient membrane fusion.The Journal of biological chemistry · 2013Article
- Class C ABC transporters andCellular logisticsArticle
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Yeast vacuole fusion requires the formation of SNARE bundles between membranes. Although the function of vacuolar SNAREs is controlled in part by regulatory lipids, the exact role of the membrane in regulating fusion remains unclear. Because SNAREs are membrane-anchored and transmit the force required for fusion to the bilayer, we hypothesized that the lipid composition and curvature of the membrane aid in controlling fusion. Here, we examined the effect of altering membrane fluidity and curvature on the functionality of fusion-incompetent SNARE mutants that are thought to generate insufficient force to trigger the hemifusion-fusion transition. The hemifusion-fusion transition was inhibited by disrupting the 3Q:1R stoichiometry of SNARE bundles with the mutant SNARE Vam7p(Q283R) . Similarly, replacing the transmembrane domain of the syntaxin homolog Vam3p with a lipid anchor allowed hemifusion, but not content mixing. Hemifusion-stalled reactions containing either of the SNARE mutants were stimulated to fuse with chlorpromazine, an amphipathic molecule that alters membrane fluidity and curvature. The activity of mutant SNAREs was also rescued by the overexpression of SNAREs, thus multiplying the force transferred to the membrane. Thus, we conclude that either increasing membrane fluidity, or multiplying SNARE-generated energy restored the fusogenicity of mutant SNAREs that are stalled at hemifusion. We also found that regulatory lipids differentially modulated the complex formation of wild-type SNAREs. Together, these data indicate that the physical properties and the lipid composition of the membrane affect the function of SNAREs in promoting the hemifusion-fusion transition.
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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.