<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>11(7)</volume><submitter>Ossareh-Nazari B</submitter><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.</pubmed_abstract><journal>EMBO reports</journal><pagination>548-54</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC2897114</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Cdc48 and Ufd3, new partners of the ubiquitin protease Ubp3, are required for ribophagy.</pubmed_title><pmcid>PMC2897114</pmcid><pubmed_authors>Schaeffer C</pubmed_authors><pubmed_authors>Delalande F</pubmed_authors><pubmed_authors>Van Dorsselaer A</pubmed_authors><pubmed_authors>Dargemont C</pubmed_authors><pubmed_authors>Cohen M</pubmed_authors><pubmed_authors>Dokudovskaya S</pubmed_authors><pubmed_authors>Bonizec M</pubmed_authors><pubmed_authors>Ossareh-Nazari B</pubmed_authors></additional><is_claimable>false</is_claimable><name>Cdc48 and Ufd3, new partners of the ubiquitin protease Ubp3, are required for ribophagy.</name><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.</description><dates><release>2010-01-01T00:00:00Z</release><publication>2010 Jul</publication><modification>2025-04-05T12:23:21.949Z</modification><creation>2019-03-27T00:32:07Z</creation></dates><accession>S-EPMC2897114</accession><cross_references><pubmed>20508643</pubmed><doi>10.1038/embor.2010.74</doi></cross_references></HashMap>