ArticleMolecular biology of the cell2011
Subunit organization and Rab interactions of Vps-C protein complexes that control endolysosomal membrane traffic.
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 79 papers.
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79 citing papers in PubMed.
- Multiple overlapping SNARE complexes drive endosome maturation in Drosophila nephrocytes.Nature communications · 2026Article
- Endosomes as central hubs of interorganellar communication and cellular homeostasis.Protein & cell · 2026Review
- Mutations in VPS18 lead to a neutrophil maturation defect associated with disturbed vesicle homeostasis.Cell death & disease · 2026Article
- ThemSphere · 2025Article
- Research progress on protein tyrosine phosphatase A from Mycobacterium tuberculosis.Frontiers in immunology · 2025Review
- A comparative analysis of paxillin and Hic-5 proximity interactomes.Cytoskeleton (Hoboken, N.J.) · 2025Article
- Structure of the endosomal CORVET tethering complex.Nature communications · 2024Article
- Regulation of Endosomal Trafficking by Rab7 and Its Effectors in Neurons: Clues from Charcot-Marie-Tooth 2B Disease.Biomolecules · 2023Review
- Human gasdermin D and MLKL disrupt mitochondria, endocytic traffic and TORC1 signalling in budding yeast.Open biology · 2023Article
- The critical role of the endolysosomal system in cerebral ischemia.Neural regeneration research · 2023Review
- Vesicle trafficking and vesicle fusion: mechanisms, biological functions, and their implications for potential disease therapy.Molecular biomedicine · 2022Review
- Article
- Arabidopsis HOPS subunit VPS41 carries out plant-specific roles in vacuolar transport and vegetative growth.Plant physiology · 2022Article
- Vision and sensorimotor defects associated with loss of Vps11 function in a zebrafish model of genetic leukoencephalopathy.Scientific reports · 2022Article
- Subunit exchange among endolysosomal tethering complexes is linked to contact site formation at the vacuole.Molecular biology of the cell · 2021Article
- 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
- FOXM1D potentiates PKM2-mediated tumor glycolysis and angiogenesis.Molecular oncology · 2021Article
- ORF3a of the COVID-19 virus SARS-CoV-2 blocks HOPS complex-mediated assembly of the SNARE complex required for autolysosome formation.Developmental cell · 2021Article
- Article
- AP-3 vesicle uncoating occurs after HOPS-dependent vacuole tethering.The EMBO journal · 2020Article
19 more citing papers are in PubMed but not listed here.
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8 authors.
Funding
Abstract
Traffic through late endolysosomal compartments is regulated by sequential signaling of small G proteins of the Rab5 and Rab7 families. The Saccharomyces cerevisiae Vps-C protein complexes CORVET (class C core vacuole/endosome tethering complex) and HOPS (homotypic fusion and protein transport) interact with endolysosomal Rabs to coordinate their signaling activities. To better understand these large and intricate complexes, we performed interaction surveys to assemble domain-level interaction topologies for the eight Vps-C subunits. We identified numerous intersubunit interactions and up to six Rab-binding sites. Functional modules coordinate the major Rab interactions within CORVET and HOPS. The CORVET-specific subunits, Vps3 and Vps8, form a subcomplex and physically and genetically interact with the Rab5 orthologue Vps21. The HOPS-specific subunits, Vps39 and Vps41, also form a subcomplex. Both subunits bind the Rab7 orthologue Ypt7, but with distinct nucleotide specificities. The in vivo functions of four RING-like domains within Vps-C subunits were analyzed and shown to have distinct functions in endolysosomal transport. Finally, we show that the CORVET- and HOPS-specific subunits Vps3 and Vps39 bind the Vps-C core through a common region within the Vps11 C-terminal domain (CTD). Biochemical and genetic experiments demonstrate the importance of these regions, revealing the Vps11 CTD as a key integrator of Vps-C complex assembly, Rab signaling, and endosomal and lysosomal traffic.
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