ArticleThe Journal of biological chemistry2008
DOA1/UFD3 plays a role in sorting ubiquitinated membrane proteins into multivesicular bodies.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 54 citations in OpenAlex.
- PLAA/UFD-3 regulates P-bodies through its intrinsic disordered domain.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Targeting of client proteins to the VCP/p97/Cdc48 unfolding machine.Frontiers in molecular biosciences · 2023Review
- The AAA-ATPase ATAD1 and its partners promote degradation of desmin intermediate filaments in muscle.EMBO reports · 2022Article
- Endosome and Golgi-associated degradation (EGAD) of membrane proteins regulates sphingolipid metabolism.The EMBO journal · 2019Article
- Genome Wide Analysis of WD40 Proteins in Saccharomyces cerevisiae and Their Orthologs in Candida albicans.The protein journal · 2019Article
- Cdc48 and ubiquilins confer selective anterograde protein sorting and entry into the multivesicular body in yeast.Molecular biology of the cell · 2018Article
- Monoubiquitination of syntaxin 3 leads to retrieval from the basolateral plasma membrane and facilitates cargo recruitment to exosomes.Molecular biology of the cell · 2017Article
- PLAA Mutations Cause a Lethal Infantile Epileptic Encephalopathy by Disrupting Ubiquitin-Mediated Endolysosomal Degradation of Synaptic Proteins.American journal of human genetics · 2017Article
- VCP/p97 cooperates with YOD1, UBXD1 and PLAA to drive clearance of ruptured lysosomes by autophagy.The EMBO journal · 2017Article
- A Mighty "Protein Extractor" of the Cell: Structure and Function of the p97/CDC48 ATPase.Frontiers in molecular biosciences · 2017Review
- Ring of Change: CDC48/p97 Drives Protein Dynamics at Chromatin.Frontiers in genetics · 2016Review
- Article
- A family of tetraspans organizes cargo for sorting into multivesicular bodies.Developmental cell · 2015Article
- Ubiquitin binding by the CUE domain promotes endosomal localization of the Rab5 GEF Vps9.Molecular biology of the cell · 2015Article
- The yeast Alix homolog Bro1 functions as a ubiquitin receptor for protein sorting into multivesicular endosomes.Developmental cell · 2013Article
- Class E compartments form in response to ESCRT dysfunction in yeast due to hyperactivity of the Vps21 Rab GTPase.Journal of cell science · 2012Article
- Cargo ubiquitination is essential for multivesicular body intralumenal vesicle formation.EMBO reports · 2012Article
- Cassette series designed for live-cell imaging of proteins and high-resolution techniques in yeast.Yeast (Chichester, England) · 2012Article
- The ubiquitin regulatory X (UBX) domain-containing protein TUG regulates the p97 ATPase and resides at the endoplasmic reticulum-golgi intermediate compartment.The Journal of biological chemistry · 2012Article
- Emerging functions of the VCP/p97 AAA-ATPase in the ubiquitin system.Nature cell biology · 2012Review
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Ubiquitin (Ub) is a sorting signal that targets integral membrane proteins to the interior of the vacuole/lysosome by directing them into lumenal vesicles of multivesicular bodies (MVBs). The Vps27-Hse1 complex, which is homologous to the Hrs-STAM complex in mammalian cells, serves as a Ub-sorting receptor at the surface of early endosomes. We have found that Hse1 interacts with Doa1/Ufd3. Doa1 is known to interact with Cdc48/p97 and Ub and is required for maintaining Ub levels. We find that the Hse1 Src homology 3 domain binds directly to the central PFU domain of Doa1. Mutations in Doa1 that block Hse1 binding but not Ub binding do not alter Ub levels but do result in the missorting of the MVB cargo GFP-Cps1. Loss of Doa1 also causes a synthetic growth defect when combined with loss of Vps27. Unlike the loss of Doa1 alone, the doa1Delta vps27Delta double mutant phenotype is not suppressed by Ub overexpression, demonstrating that the effect is not due to indirect consequence of lowered Ub levels. Loss of Doa1 results in a defect in the accumulation of GFP-Ub within yeast vacuoles, implying that there is a reduction in the flux of ubiquitinated membrane proteins through the MVB pathway. This defect was also reflected by an inability to properly sort Vph1-GFP-Ub, a modified subunit of the multiprotein vacuolar ATPase complex, which carries an in-frame fusion of Ub as an MVB sorting signal. These results reveal novel roles for Doa1 in helping to process ubiquitinated membrane proteins for sorting into MVBs.
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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.