ArticleJournal of cell science2013
Doa4 function in ILV budding is restricted through its interaction with the Vps20 subunit of ESCRT-III.
Article in Journal of cell science, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 22 citations in OpenAlex.
- Wbm0152, an outer membrane lipoprotein of the Wolbachia endosymbiont of Brugia malayi, inhibits yeast ESCRT complex activity.PLoS pathogens · 2025Article
- ESCRTing the RABs through conversion.Biochemical Society transactions · 2025Review
- Bro1 binds the Vps20 subunit of ESCRT-III and promotes ESCRT-III regulation by Doa4.Traffic (Copenhagen, Denmark) · 2022Article
- Interactions of ubiquitin and CHMP5 with the V domain of HD-PTP reveals role for regulation of Vps4 ATPase.Molecular biology of the cell · 2021Article
- Bro1 stimulates Vps4 to promote intralumenal vesicle formation during multivesicular body biogenesis.The Journal of cell biology · 2021Article
- Vacuolar H+-ATPase dysfunction rescues intralumenal vesicle cargo sorting in yeast lacking PI(3,5)P2 or Doa4.Journal of cell science · 2021Article
- The ubiquitin hydrolase Doa4 directly binds Snf7 to inhibit recruitment of ESCRT-III remodeling factors inJournal of cell science · 2020Article
- Article
- ESCRT-dependent cargo sorting at multivesicular endosomes.Seminars in cell & developmental biology · 2018Review
- ESCRT-mediated vesicle concatenation in plant endosomes.The Journal of cell biology · 2017Article
- Regulation of yeast ESCRT-III membrane scission activity by the Doa4 ubiquitin hydrolase.Molecular biology of the cell · 2017Article
- Host ESCRT proteins are required for bromovirus RNA replication compartment assembly and function.PLoS pathogens · 2015Article
- Review
- Coordinated binding of Vps4 to ESCRT-III drives membrane neck constriction during MVB vesicle formation.The Journal of cell biology · 2014Article
- Ubiquitin-dependent sorting in endocytosis.Cold Spring Harbor perspectives in biology · 2014Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Assembly of the endosomal sorting complex required for transport (ESCRT)-III executes the formation of intralumenal vesicles (ILVs) at endosomes. Repeated cycles of ESCRT-III function requires disassembly of the complex by Vps4, an ATPase with a microtubule interaction and trafficking (MIT) domain that binds MIT-interacting motifs (MIM1 or MIM2) in ESCRT-III subunits. We identified a putative MIT domain at the N-terminus of Doa4, which is the ubiquitin (Ub) hydrolase in Saccharomyces cerevisiae that deubiquitinates ILV cargo proteins. The Doa4 N-terminus is predicted to have the α-helical structure common to MIT domains, and it binds directly to a MIM1-like sequence in the Vps20 subunit of ESCRT-III. Disrupting this interaction does not prevent endosomal localization of Doa4 but enhances the defect in ILV cargo protein deubiquitination observed in cells lacking Bro1, which is an ESCRT-III effector protein that stimulates Doa4 catalytic activity. Deletion of the BRO1 gene (bro1Δ) blocks ILV budding, but ILV budding was rescued upon disrupting the interaction between Vps20 and Doa4. This rescue in ILV biogenesis requires Doa4 expression but is independent of its Ub hydrolase activity. Thus, binding of Vps20 to the Doa4 N-terminus inhibits a non-catalytic function of Doa4 that promotes ILV formation.
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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.