ArticleMolecular biology of the cell2011
HOPS drives vacuole fusion by binding the vacuolar SNARE complex and the Vam7 PX domain via two distinct sites.
Article in Molecular biology of the cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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Who cites it
49 citing papers in PubMed, 88 citations in OpenAlex.
- A primordial synaptotagmin-independent function of complexin in regulated exocytosis.Nature communications · 2026Article
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- Neuronal SNARE complex assembly guided by Munc18-1 and Munc13-1.FEBS open bio · 2022Review
- Article
- The Rab7 effector WDR91 promotes autophagy-lysosome degradation in neurons by regulating lysosome fusion.The Journal of cell biology · 2021Article
- Redirecting Vesicular Transport to Improve Nonviral Delivery of Molecular Cargo.Advanced biosystems · 2020Article
- HOPS recognizes each SNARE, assembling ternaryeLife · 2020Article
- Intracellular Vesicle Fusion Requires a Membrane-Destabilizing Peptide Located at the Juxtamembrane Region of the v-SNARE.Cell reports · 2019Article
- The inner workings of intracellular heterotypic and homotypic membrane fusion mechanisms.Journal of biosciences · 2019Article
- The road to lysosome-related organelles: Insights from Hermansky-Pudlak syndrome and other rare diseases.Traffic (Copenhagen, Denmark) · 2019Review
- Rab5-independent activation and function of yeast Rab7-like protein, Ypt7p, in the AP-3 pathway.PloS one · 2019Article
- Reconstitution reveals Ykt6 as the autophagosomal SNARE in autophagosome-vacuole fusion.The Journal of cell biology · 2018Article
- Non-canonical role of the SNARE protein Ykt6 in autophagosome-lysosome fusion.PLoS genetics · 2018Article
- Sec17 (α-SNAP) and an SM-tethering complex regulate the outcome of SNARE zippering in vitro and in vivo.eLife · 2017Article
- A short region upstream of the yeast vacuolar Qa-SNARE heptad-repeats promotes membrane fusion through enhanced SNARE complex assembly.Molecular biology of the cell · 2017Article
- Article
- HOPS catalyzes the interdependent assembly of each vacuolar SNARE into a SNARE complex.Molecular biology of the cell · 2017Article
- A HOPS Protein, MoVps41, Is Crucially Important for Vacuolar Morphogenesis, Vegetative Growth, Reproduction and Virulence inFrontiers in plant science · 2017Article
- 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
- Chaperoning SNARE assembly and disassembly.Nature reviews. Molecular cell biology · 2016Review
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Membrane fusion within the endomembrane system follows a defined order of events: membrane tethering, mediated by Rabs and tethers, assembly of soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein receptor (SNARE) complexes, and lipid bilayer mixing. Here we present evidence that the vacuolar HOPS tethering complex controls fusion through specific interactions with the vacuolar SNARE complex (consisting of Vam3, Vam7, Vti1, and Nyv1) and the N-terminal domains of Vam7 and Vam3. We show that homotypic fusion and protein sorting (HOPS) binds Vam7 via its subunits Vps16 and Vps18. In addition, we observed that Vps16, Vps18, and the Sec1/Munc18 protein Vps33, which is also part of the HOPS complex, bind to the Q-SNARE complex. In agreement with this observation, HOPS-stimulated fusion was inhibited if HOPS was preincubated with the minimal Q-SNARE complex. Importantly, artificial targeting of Vam7 without its PX domain to membranes rescued vacuole morphology in vivo, but resulted in a cytokinesis defect if the N-terminal domain of Vam3 was also removed. Our data thus support a model of HOPS-controlled membrane fusion by recognizing different elements of the SNARE complex.
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