ArticleeLife2022
Structure of the HOPS tethering complex, a lysosomal membrane fusion machinery.
Article in eLife, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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Who cites it
51 citing papers in PubMed.
- Retromer mediates Ypt7-dependent lipid droplet internalization.Cell reports · 2026Article
- A GUV-based assay to reconstitute membrane tethering in vitro.Molecular biology of the cell · 2026Article
- Review
- Crystal structures of Fsc1, a novel autophagy factor that mediates autophagosome-vacuole fusion in fission yeast.Acta crystallographica. Section D, Structural biology · 2026Article
- Functional assembly of the Qc-SNARE with Sec18 and Sec17 on membranes.Molecular biology of the cell · 2026Article
- NPC1 trafficking via VPS41-dependent LAMP carriers regulates endosomal cholesterol homeostasis.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- AoVps18 regulates sporulation, trap morphogenesis, and nematode predation by modulating vacuole assembly and attractant synthesis inVirulence · 2025Article
- Regulation of vacuole fusion in stomata by dephosphorylation of the HOPS subunit VPS39.The Plant journal : for cell and molecular biology · 2025Article
- Mammalian innate antiviral defenses: beyond interferon.Journal of virology · 2025Review
- Bergeyella cardium variant induces a unique cytoplasmic vacuolization cell death floatptosis in macrophage.Cell discovery · 2025Article
- Cysteine reactivity profiling identifies host regulators ofbioRxiv : the preprint server for biology · 2025Article
- SNARE disassembly requires Sec18/NSF side loading.Nature structural & molecular biology · 2025Article
- Spatio-temporal processes in autophagosome-lysosome fusion.Medical review (2021) · 2025Review
- ThemSphere · 2025Article
- Sec18 ATP hydrolysis selectively releases Sec17 fromMolecular biology of the cell · 2025Article
- SNARE disassembly requires Sec18/NSF side-loading.bioRxiv : the preprint server for biology · 2025Article
- Endocytic tethers modulate unconventional GAPDH secretion.Cell surface (Amsterdam, Netherlands) · 2025Article
- Hemifusomes and interacting proteolipid nanodroplets mediate multi-vesicular body formation.Nature communications · 2025Article
- Hastened Fusion-Dependent Endosomal Escape Improves Activity of Delivered Enzyme Cargo.ACS central science · 2025Article
- RAB-10 cooperates with EHBP-1 to capture vesicular carriers during post-Golgi exocytic trafficking.The Journal of cell biology · 2025Article
Corrections and comments
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Authors and funding
13 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lysosomes are essential for cellular recycling, nutrient signaling, autophagy, and pathogenic bacteria and viruses invasion. Lysosomal fusion is fundamental to cell survival and requires HOPS, a conserved heterohexameric tethering complex. On the membranes to be fused, HOPS binds small membrane-associated GTPases and assembles SNAREs for fusion, but how the complex fulfills its function remained speculative. Here, we used cryo-electron microscopy to reveal the structure of HOPS. Unlike previously reported, significant flexibility of HOPS is confined to its extremities, where GTPase binding occurs. The SNARE-binding module is firmly attached to the core, therefore, ideally positioned between the membranes to catalyze fusion. Our data suggest a model for how HOPS fulfills its dual functionality of tethering and fusion and indicate why it is an essential part of the membrane fusion machinery.
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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 Socratic graph.