ArticleProceedings of the National Academy of Sciences of the United States of America2007
Trans-SNARE complex assembly and yeast vacuole membrane fusion.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.
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Who cites it
55 citing papers in PubMed, 83 citations in OpenAlex.
- Plasma membrane CYBDOM proteins catalyse apoplastic AsA regeneration and interact with RbohD to activate autophagy and drought tolerance in plants.Nature plants · 2025Article
- Loss of the HOPS complex disrupts early-to-late endosome transition, impairs endosomal recycling and induces accumulation of amphisomes.Molecular biology of the cell · 2024Article
- SNARE Protein Snc1 Is Essential for Vesicle Trafficking, Membrane Fusion and Protein Secretion in Fungi.Cells · 2023Review
- Sec18 supports membrane fusion by promoting Sec17 membrane association.Molecular biology of the cell · 2022Article
- Asymmetric Rab activation of vacuolar HOPS to catalyze SNARE complex assembly.Molecular biology of the cell · 2020Article
- HOPS recognizes each SNARE, assembling ternaryeLife · 2020Article
- Copper blocks V-ATPase activity and SNARE complex formation to inhibit yeast vacuole fusion.Traffic (Copenhagen, Denmark) · 2019Article
- Tethering guides fusion-competentProceedings of the National Academy of Sciences of the United States of America · 2019Article
- The Participation of Regulatory Lipids in Vacuole Homotypic Fusion.Trends in biochemical sciences · 2019Review
- Munc18 and Munc13 serve as a functional template to orchestrate neuronal SNARE complex assembly.Nature communications · 2019Article
- HOPS catalyzes the interdependent assembly of each vacuolar SNARE into a SNARE complex.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
- The Secret Life of Tethers: The Role of Tethering Factors in SNARE Complex Regulation.Frontiers in cell and developmental biology · 2016Review
- The Exocyst Subunit Sec6 Interacts with Assembled Exocytic SNARE Complexes.The Journal of biological chemistry · 2015Article
- SNAREs support atlastin-mediated homotypic ER fusion in Saccharomyces cerevisiae.The Journal of cell biology · 2015Article
- The membrane domain of vacuolar H(+)ATPase: a crucial player in neurotransmitter exocytotic release.Cellular and molecular life sciences : CMLS · 2015Review
- Vacuolar SNARE protein transmembrane domains serve as nonspecific membrane anchors with unequal roles in lipid mixing.The Journal of biological chemistry · 2015Article
- Sec17 can trigger fusion of trans-SNARE paired membranes without Sec18.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Vibrio effector protein VopQ inhibits fusion of V-ATPase-containing membranes.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
cis-SNARE complexes (anchored in one membrane) are disassembled by Sec17p (alpha-SNAP) and Sec18p (NSF), permitting the unpaired SNAREs to assemble in trans. We now report a direct assay of trans-SNARE complex formation during yeast vacuole docking. SNARE complex assembly and fusion is promoted by high concentrations of the SNARE Vam7p or Nyv1p or by addition of HOPS (homotypic fusion and vacuole protein sorting), a Ypt7p (Rab)-effector complex with a Sec1/Munc18-family subunit. Inhibitors that target Ypt7p, HOPS, or key regulatory lipids prevent trans-SNARE complex assembly and ensuing fusion. Strikingly, the lipid ligand MED (myristoylated alanine-rich C kinase substrate effector domain) or elevated concentrations of Sec17p, which can displace HOPS from SNARE complexes, permit full trans-SNARE pairing but block fusion. These findings suggest that efficient fusion requires trans-SNARE complex associations with factors such as HOPS and subsequent regulated lipid rearrangements.
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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.