ArticleThe Journal of biological chemistry2014
Structural identification of the Vps18 β-propeller reveals a critical role in the HOPS complex stability and function.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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Who cites it
11 citing papers in PubMed, 18 citations in OpenAlex.
- Mutations in VPS18 lead to a neutrophil maturation defect associated with disturbed vesicle homeostasis.Cell death & disease · 2026Article
- Targeting VPS18 hampers retromer trafficking of PD-L1 and augments immunotherapy.Science advances · 2024Article
- An initial HOPS-mediated fusion event is critical for autophagosome transport initiation from the axon terminal.Autophagy · 2024Article
- Article
- Molecular structures and function of the autophagosome-lysosome fusion machinery.Autophagy reports · 2024Article
- A Novel Homozygous VPS11 Variant May Cause Generalized Dystonia.Annals of neurology · 2021Article
- Mucopolysaccharidosis-Plus Syndrome.International journal of molecular sciences · 2020Article
- Vps11 and Vps18 of Vps-C membrane traffic complexes are E3 ubiquitin ligases and fine-tune signalling.Nature communications · 2019Article
- VPS18 recruits VPS41 to the human HOPS complex via a RING-RING interaction.The Biochemical journal · 2017Article
- Multiple Roles of the Small GTPase Rab7.Cells · 2016Review
- Coat/Tether Interactions-Exception or Rule?Frontiers in cell and developmental biology · 2016Review
Corrections and comments
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Authors and funding
11 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Membrane fusion at the vacuole, the lysosome equivalent in yeast, requires the HOPS tethering complex, which is recruited by the Rab7 GTPase Ypt7. HOPS provides a template for the assembly of SNAREs and thus likely confers fusion at a distinct position on vacuoles. Five of the six subunits in HOPS have a similar domain prediction with strong similarity to COPII subunits and nuclear porins. Here, we show that Vps18 indeed has a seven-bladed β-propeller as its N-terminal domain by revealing its structure at 2.14 Å. The Vps18 N-terminal domain can interact with the N-terminal part of Vps11 and also binds to lipids. Although deletion of the Vps18 N-terminal domain does not preclude HOPS assembly, as revealed by negative stain electron microscopy, the complex is instable and cannot support membrane fusion in vitro. We thus conclude that the β-propeller of Vps18 is required for HOPS stability and function and that it can serve as a starting point for further structural analyses of the HOPS tethering complex.
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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.