ArticleMolecular biology of the cell2009
HOPS interacts with Apl5 at the vacuole membrane and is required for consumption of AP-3 transport vesicles.
Article in Molecular biology of the cell, 2009. 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, 81 citations in OpenAlex.
- Multiple overlapping SNARE complexes drive endosome maturation in Drosophila nephrocytes.Nature communications · 2026Article
- AP-3 and the V-ATPase modulate CTP synthase assembly through spatial association at the yeast vacuole.Molecular biology of the cell · 2026Article
- Septins associate with AP-3 to support trafficking to the vacuole/lysosome in yeast.Molecular biology of the cell · 2026Article
- AP-3 and the V-ATPase Modulate CTP Synthase Assembly Through Spatial Association at the Yeast Vacuole.bioRxiv : the preprint server for biology · 2026Article
- Septins associate with AP-3 to support trafficking to the vacuole/lysosome in yeast.bioRxiv : the preprint server for biology · 2026Article
- Gene expression and dispersion profiles associated with water consumption and general activity in grazing beef cattle.Tropical animal health and production · 2025Article
- A Set of Fluorescent Protein-Based Markers for Major Vesicle Coat Proteins in Yeast.Membranes · 2025Article
- HOPS-dependent vesicle tethering lock inhibits endolysosomal fusions and autophagosome secretion upon the loss of Syntaxin17.Science advances · 2025Article
- HOPS/CORVET tethering complexes are critical for endocytosis and protein trafficking to invasion related organelles in malaria parasites.PLoS pathogens · 2025Article
- Disordered hinge regions of the AP-3 adaptor complex promote vesicle budding from the late Golgi in yeast.Journal of cell science · 2024Article
- CORVET-specific subunit levels determine the balance between HOPS/CORVET endosomal tethering complexes.Scientific reports · 2024Article
- The TRAPP complexes: oligomeric exchange factors that activate the small GTPases Rab1 and Rab11.FEBS letters · 2023Review
- TbVps41 regulates trafficking of endocytic but not biosynthetic cargo to lysosomes of bloodstream forms of Trypanosoma brucei.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2021Article
- Neurodegenerative VPS41 variants inhibit HOPS function and mTORC1-dependent TFEB/TFE3 regulation.EMBO molecular medicine · 2021Article
- Auxilin-like protein MoSwa2 promotes effector secretion and virulence as a clathrin uncoating factor in the rice blast fungus Magnaporthe oryzae.The New phytologist · 2021Article
- Cargo Release from Myosin V Requires the Convergence of Parallel Pathways that Phosphorylate and Ubiquitylate the Cargo Adaptor.Current biology : CB · 2020Article
- AP-3 vesicle uncoating occurs after HOPS-dependent vacuole tethering.The EMBO journal · 2020Article
- Spatiotemporal dissection of theJournal of cell science · 2019Article
- Vps8 overexpression inhibits HOPS-dependent trafficking routes by outcompeting Vps41/Lt.eLife · 2019Article
- Budding Yeast Has a Minimal Endomembrane System.Developmental cell · 2018Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Adaptor protein complexes (APs) are evolutionarily conserved heterotetramers that couple cargo selection to the formation of highly curved membranes during vesicle budding. In Saccharomyces cerevisiae, AP-3 mediates vesicle traffic from the late Golgi to the vacuolar lysosome. The HOPS subunit Vps41 is one of the few proteins reported to have a specific role in AP-3 traffic, yet its function remains undefined. We now show that although the AP-3 delta subunit, Apl5, binds Vps41 directly, this interaction occurs preferentially within the context of the HOPS docking complex. Fluorescence microscopy indicates that Vps41 and other HOPS subunits do not detectably colocalize with AP-3 at the late Golgi or on post-Golgi (Sec7-negative) vesicles. Vps41 and HOPS do, however, transiently colocalize with AP-3 vesicles when these vesicles dock at the vacuole membrane. In cells with mutations in HOPS subunits or the vacuole SNARE Vam3, AP-3 shifts from the cytosol to a membrane fraction. Fluorescence microscopy suggests that this fraction consists of post-Golgi AP-3 vesicles that have failed to dock or fuse at the vacuole membrane. We propose that AP-3 remains associated with budded vesicles, interacts with Vps41 and HOPS upon vesicle docking at the vacuole, and finally dissociates during docking or fusion.
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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.