ArticleMolecular biology of the cell2008
HOPS proofreads the trans-SNARE complex for yeast vacuole fusion.
Article in Molecular biology of the cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers.
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Who cites it
74 citing papers in PubMed.
- Engineering Yeast Extracellular Vesicle Biogenesis Through Rewiring Membrane Trafficking Pathways.Microbial biotechnology · 2026Article
- 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
- SNARE Proteins in Synaptic Vesicle Fusion.Advances in neurobiology · 2023Article
- Sec18 supports membrane fusion by promoting Sec17 membrane association.Molecular biology of the cell · 2022Article
- Emerging Concepts in Defective Macrophage Phagocytosis in Cystic Fibrosis.International journal of molecular sciences · 2022Review
- Fusion with wild-type SNARE domains is controlled by juxtamembrane domains, transmembrane anchors, and Sec17.Molecular biology of the cell · 2022Article
- Molecular mechanisms of endomembrane trafficking in plants.The Plant cell · 2022Review
- 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
- The road to lysosome-related organelles: Insights from Hermansky-Pudlak syndrome and other rare diseases.Traffic (Copenhagen, Denmark) · 2019Review
- 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
- Phosphoinositides control the localization of HOPS subunit VPS41, which together with VPS33 mediates vacuole fusion in plants.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Solution NMR of SNAREs, complexin and α-synuclein in association with membrane-mimetics.Progress in nuclear magnetic resonance spectroscopy · 2018Review
- Sequential actions of phosphatidylinositol phosphates regulate phagosome-lysosome fusion.Molecular biology of the cell · 2018Article
- Sec17 (α-SNAP) and an SM-tethering complex regulate the outcome of SNARE zippering in vitro and in vivo.eLife · 2017Article
- Article
- How and why intralumenal membrane fragments form during vacuolar lysosome fusion.Molecular biology of the cell · 2017Article
- Multivalent Rab interactions determine tether-mediated membrane fusion.Molecular biology of the cell · 2017Article
14 more citing papers are in PubMed but not listed here.
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3 authors.
Funding
Abstract
The fusion of yeast vacuoles, like other organelles, requires a Rab-family guanosine triphosphatase (Ypt7p), a Rab effector and Sec1/Munc18 (SM) complex termed HOPS (homotypic fusion and vacuole protein sorting), and soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs). The central 0-layer of the four bundled vacuolar SNAREs requires the wild-type three glutaminyl (Q) and one arginyl (R) residues for optimal fusion. Alterations of this layer dramatically increase the K(m) value for SNAREs to assemble trans-SNARE complexes and to fuse. We now find that added purified HOPS complex strongly suppresses the fusion of vacuoles bearing 0-layer alterations, but it has little effect on the fusion of vacuoles with wild-type SNAREs. HOPS proofreads at two levels, inhibiting the formation of trans-SNARE complexes with altered 0-layers and suppressing the ability of these mismatched 0-layer trans-SNARE complexes to support membrane fusion. HOPS proofreading also extends to other parts of the SNARE complex, because it suppresses the fusion of trans-SNARE complexes formed without the N-terminal Phox homology domain of Vam7p (Q(c)). Unlike some other SM proteins, HOPS proofreading does not require the Vam3p (Q(a)) N-terminal domain. HOPS thus proofreads SNARE domain and N-terminal domain structures and regulates the fusion capacity of trans-SNARE complexes, only allowing full function for wild-type SNARE configurations. This is the most direct evidence to date that HOPS is directly involved in the fusion event.
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