ArticleeLife2014
A distinct tethering step is vital for vacuole membrane fusion.
Article in eLife, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 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
52 citing papers in PubMed, 65 citations in OpenAlex.
- Multiple overlapping SNARE complexes drive endosome maturation in Drosophila nephrocytes.Nature communications · 2026Article
- Functional assembly of the Qc-SNARE with Sec18 and Sec17 on membranes.Molecular biology of the cell · 2026Article
- Sec18 ATP hydrolysis selectively releases Sec17 fromMolecular biology of the cell · 2025Article
- Structure of the endosomal CORVET tethering complex.Nature communications · 2024Article
- The GTPase activating protein Gyp7 regulates Rab7/Ypt7 activity on late endosomes.The Journal of cell biology · 2024Article
- Sec18 binds the tethering/SM complex HOPS to engage the Qc-SNARE for membrane fusion.Molecular biology of the cell · 2024Article
- MARCKS Effector Domain, a reversible lipid ligand, illuminates late stages of membrane fusion.Molecular biology of the cell · 2023Article
- Human atlastins are sufficient to drive the fusion of liposomes with a physiological lipid composition.The Journal of cell biology · 2023Article
- PI3P regulates multiple stages of membrane fusion.Molecular biology of the cell · 2023Article
- Sec18 supports membrane fusion by promoting Sec17 membrane association.Molecular biology of the cell · 2022Article
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- Molecular Mechanisms Underlying Neurotransmitter Release.Annual review of biophysics · 2022Review
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- Organelle tethering, pore formation and SNARE compensation in the late endocytic pathway.Journal of cell science · 2021Article
- Sec17/Sec18 can support membrane fusion without help from completion of SNARE zippering.eLife · 2021Article
- Synaptotagmin-1-, Munc18-1-, and Munc13-1-dependent liposome fusion with a few neuronal SNAREs.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- A kinase cascade on the yeast lysosomal vacuole regulates its membrane dynamics: conserved kinase Env7 is phosphorylated by casein kinase Yck3.The Journal of biological chemistry · 2020Article
- Roles of Mso1 and the SM protein Sec1 in efficient vesicle fusion during fission yeast cytokinesis.Molecular biology of the cell · 2020Article
- Article
- Asymmetric Rab activation of vacuolar HOPS to catalyze SNARE complex assembly.Molecular biology of the cell · 2020Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Past experiments with reconstituted proteoliposomes, employing assays that infer membrane fusion from fluorescent lipid dequenching, have suggested that vacuolar SNAREs alone suffice to catalyze membrane fusion in vitro. While we could replicate these results, we detected very little fusion with the more rigorous assay of lumenal compartment mixing. Exploring the discrepancies between lipid-dequenching and content-mixing assays, we surprisingly found that the disposition of the fluorescent lipids with respect to SNAREs had a striking effect. Without other proteins, the association of SNAREs in trans causes lipid dequenching that cannot be ascribed to fusion or hemifusion. Tethering of the SNARE-bearing proteoliposomes was required for efficient lumenal compartment mixing. While the physiological HOPS tethering complex caused a few-fold increase of trans-SNARE association, the rate of content mixing increased more than 100-fold. Thus tethering has a role in promoting membrane fusion that extends beyond simply increasing the amount of total trans-SNARE complex.
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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.