ArticleMolecular biology of the cell2013
The tethering complex HOPS catalyzes assembly of the soluble SNARE Vam7 into fusogenic trans-SNARE complexes.
Article in Molecular biology of the cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed, 63 citations in OpenAlex.
- 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
- After their membrane assembly, Sec18 (NSF) and Sec17 (SNAP) promote membrane fusion.Molecular biology of the cell · 2024Article
- Membrane fusion reactions limited by defective SNARE zippering or stiff lipid fatty acyl composition have distinct requirements for Sec17, Sec18, and adenine nucleotide.bioRxiv : the preprint server for biology · 2024Article
- Sec18 binds the tethering/SM complex HOPS to engage the Qc-SNARE for membrane fusion.Molecular biology of the cell · 2024Article
- 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
- Model-based inference of a dual role for HOPS in regulating guard cell vacuole fusion.In silico plants · 2024Article
- Model-based inference of a plant-specific dual role for HOPS in regulating guard cell vacuole fusion.bioRxiv : the preprint server for biology · 2023Article
- MARCKS Effector Domain, a reversible lipid ligand, illuminates late stages of membrane fusion.Molecular biology of the cell · 2023Article
- Efficient fusion requires a membrane anchor on the vacuolar Qa-SNARE.Molecular biology of the cell · 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
- Mechanisms regulating the sorting of soluble lysosomal proteins.Bioscience reports · 2022Review
- Fusion with wild-type SNARE domains is controlled by juxtamembrane domains, transmembrane anchors, and Sec17.Molecular biology of the cell · 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
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- An active tethering mechanism controls the fate of vesicles.Nature communications · 2021Article
- Sec17/Sec18 can support membrane fusion without help from completion of SNARE zippering.eLife · 2021Article
- Asymmetric Rab activation of vacuolar HOPS to catalyze SNARE complex assembly.Molecular biology of the cell · 2020Article
- A Rab prenyl membrane-anchor allows effector recognition to be regulated by guanine nucleotide.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
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2 authors at 1 institution in 1 country.
Funding
Abstract
The fusion of yeast vacuolar membranes depends on the disassembly of cis-soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complexes and the subsequent reassembly of new SNARE complexes in trans. The disassembly of cis-SNARE complexes by Sec17/Sec18p releases the soluble SNARE Vam7p from vacuolar membranes. Consequently, Vam7p needs to be recruited to the membrane at future sites of fusion to allow the formation of trans-SNARE complexes. The multisubunit tethering homotypic fusion and vacuole protein sorting (HOPS) complex, which is essential for the fusion of vacuolar membranes, was previously shown to have direct affinity for Vam7p. The functional significance of this interaction, however, has been unclear. Using a fully reconstituted in vitro fusion reaction, we now show that HOPS facilitates membrane fusion by recruiting Vam7p for fusion. In the presence of HOPS, unlike with other tethering agents, very low levels of added Vam7p suffice to induce vigorous fusion. This is a specific recruitment of Vam7p rather than an indirect stimulation of SNARE complex formation through tethering, as HOPS does not facilitate fusion with a low amount of a soluble form of another vacuolar SNARE, Vti1p. Our findings establish yet another function among the multiple tasks that HOPS performs to catalyze the fusion of yeast vacuoles.
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