ArticleThe EMBO journal2004
A soluble SNARE drives rapid docking, bypassing ATP and Sec17/18p for vacuole fusion.
Article in The EMBO journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.
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Who cites it
65 citing papers in PubMed, 100 citations in OpenAlex.
- Functional assembly of the Qc-SNARE with Sec18 and Sec17 on membranes.Molecular biology of the cell · 2026Article
- MARCKS Effector Domain, a reversible lipid ligand, illuminates late stages of membrane fusion.Molecular biology of the cell · 2023Article
- 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
- Organelle tethering, pore formation and SNARE compensation in the late endocytic pathway.Journal of cell science · 2021Article
- Asymmetric Rab activation of vacuolar HOPS to catalyze SNARE complex assembly.Molecular biology of the cell · 2020Article
- HOPS recognizes each SNARE, assembling ternaryeLife · 2020Article
- Tethering guides fusion-competentProceedings of the National Academy of Sciences of the United States of America · 2019Article
- 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
- Cytokine exocytosis and JAK/STAT activation in theJournal of cell science · 2018Article
- The NaMolecular biology of the cell · 2018Article
- Assembly of intermediates for rapid membrane fusion.The Journal of biological chemistry · 2018Article
- Article
- Sec17 (α-SNAP) and an SM-tethering complex regulate the outcome of SNARE zippering in vitro and in vivo.eLife · 2017Article
- The Golgin protein Coy1 functions in intra-Golgi retrograde transport and interacts with the COG complex and Golgi SNAREs.Molecular biology of the cell · 2017Article
- How and why intralumenal membrane fragments form during vacuolar lysosome fusion.Molecular biology of the cell · 2017Article
- 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
- Organelle acidification negatively regulates vacuole membrane fusion in vivo.Scientific reports · 2016Article
- SNAREs support atlastin-mediated homotypic ER fusion in Saccharomyces cerevisiae.The Journal of cell biology · 2015Article
5 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Membrane fusion requires priming, the disassembly of cis-SNARE complexes by the ATP-driven chaperones Sec18/17p. Yeast vacuole priming releases Vam7p, a soluble SNARE. Vam7p reassociation during docking allows trans-SNARE pairing and fusion. We now report that recombinant Vam7p (rVam7p) enters into complex with other SNAREs in vitro and bypasses the need for Sec17p, Sec18p, and ATP. Thus, the sole essential function of vacuole priming in vitro is the release of Vam7p from cis-SNARE complexes. In 'bypass fusion', without ATP but with added rVam7p, there are sufficient unpaired vacuolar SNAREs Vam3p, Vti1p, and Nyv1p to interact with Vam7p and support fusion. However, active SNARE proteins are not sufficient for bypass fusion. rVam7p does not bypass requirements for Rho GTPases,Vps33p, Vps39p, Vps41p, calmodulin, specific lipids, or Vph1p, a subunit of the V-ATPase. With excess rVam7p, reduced levels of PI(3)P or functional Ypt7p suffice for bypass fusion. High concentrations of rVam7p allow the R-SNARE Ykt6p to substitute for Nyv1p for fusion; this functional redundancy among vacuole SNAREs may explain why nyv1delta strains lack the vacuole fragmentation seen with mutants in other fusion catalysts.
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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.