{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["11(7)"],"submitter":["Ossareh-Nazari B"],"pubmed_abstract":["Ubiquitin-dependent processes can be antagonized by substrate-specific deubiquitination enzymes involved in many cellular functions. In this study, we show that the yeast Ubp3-Bre5 deubiquitination complex interacts with both the chaperone-like Cdc48, a major actor of the ubiquitin and proteasome system, and Ufd3, a ubiquitin-binding cofactor of Cdc48. We observed that these partners are required for the Ubp3-Bre5-dependent and starvation-induced selective degradation of yeast mature ribosomes, also called ribophagy. By contrast, proteasome-dependent degradation does not participate in this process. Our data favour the idea that these factors cooperate to recognize and deubiquitinate specific substrates of ribophagy before their vacuolar degradation."],"journal":["EMBO reports"],"pagination":["548-54"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC2897114"],"repository":["biostudies-literature"],"pubmed_title":["Cdc48 and Ufd3, new partners of the ubiquitin protease Ubp3, are required for ribophagy."],"pmcid":["PMC2897114"],"pubmed_authors":["Schaeffer C","Delalande F","Van Dorsselaer A","Dargemont C","Cohen M","Dokudovskaya S","Bonizec M","Ossareh-Nazari B"],"additional_accession":[]},"is_claimable":false,"name":"Cdc48 and Ufd3, new partners of the ubiquitin protease Ubp3, are required for ribophagy.","description":"Ubiquitin-dependent processes can be antagonized by substrate-specific deubiquitination enzymes involved in many cellular functions. In this study, we show that the yeast Ubp3-Bre5 deubiquitination complex interacts with both the chaperone-like Cdc48, a major actor of the ubiquitin and proteasome system, and Ufd3, a ubiquitin-binding cofactor of Cdc48. We observed that these partners are required for the Ubp3-Bre5-dependent and starvation-induced selective degradation of yeast mature ribosomes, also called ribophagy. By contrast, proteasome-dependent degradation does not participate in this process. Our data favour the idea that these factors cooperate to recognize and deubiquitinate specific substrates of ribophagy before their vacuolar degradation.","dates":{"release":"2010-01-01T00:00:00Z","publication":"2010 Jul","modification":"2025-04-05T12:23:21.949Z","creation":"2019-03-27T00:32:07Z"},"accession":"S-EPMC2897114","cross_references":{"pubmed":["20508643"],"doi":["10.1038/embor.2010.74"]}}