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dc.rights.licenseopenen_US
hal.structure.identifierVIB-KU Leuven Center for Microbiology [Leuven, Belgium]
hal.structure.identifierDepartment of Oncology [Leuven, Belgium]
dc.contributor.authorSHERYAZDANOVA, Aidana
hal.structure.identifierLaboratoire Maladies Rares: Génétique et Métabolisme (Bordeaux) [U1211 INSERM/MRGM]
dc.contributor.authorAMOEDO, Nivea Dias
hal.structure.identifierVIB-UGent Center for Medical Biotechnology
hal.structure.identifierVIB Proteomics Core, Ghent, Belgium
dc.contributor.authorDUFOUR, Sara
hal.structure.identifierVIB-UGent Center for Medical Biotechnology
hal.structure.identifierVIB Proteomics Core, Ghent, Belgium
dc.contributor.authorIMPENS, Francis
hal.structure.identifierLaboratoire Maladies Rares: Génétique et Métabolisme (Bordeaux) [U1211 INSERM/MRGM]
dc.contributor.authorROSSIGNOL, Rodrigue
hal.structure.identifierVIB-KU Leuven Center for Microbiology [Leuven, Belgium]
hal.structure.identifierDepartment of Oncology [Leuven, Belgium]
dc.contributor.authorSABLINA, Anna
dc.date.accessioned2023-11-28T13:10:09Z
dc.date.available2023-11-28T13:10:09Z
dc.date.issued2023-10-01
dc.identifier.issn1879-260Xen_US
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/186199
dc.description.abstractEnAerobic glycolysis is a hallmark of cancer development, but this dogma has been challenged by reports showing a key role of oxidative phosphorylation (OXPHOS) in cancer cell survival. It has been proposed that increased levels of intramitochondrial proteins in cancer cells are associated with high OXPHOS activity and increased sensitivity to OXPHOS inhibitors. However, the molecular mechanisms leading to the high expression of OXPHOS proteins in cancer cells remain unknown. Multiple proteomics studies have detected the ubiquitination of intramitochondrial proteins, suggesting the contribution of the ubiquitin system to the proteostatic regulation of OXPHOS proteins. Here, we identified the ubiquitin hydrolase OTUB1 as a regulator of the mitochondrial metabolic machinery essential for lung cancer cell survival. Mitochondria-localized OTUB1 modulates respiration by inhibiting K48-linked ubiquitination and turnover of OXPHOS proteins. An increase in OTUB1 expression is commonly observed in one-third of non-small-cell lung carcinomas and is associated with high OXPHOS signatures. Moreover, OTUB1 expression highly correlates with the sensitivity of lung cancer cells to mitochondrial inhibitors.
dc.language.isoENen_US
dc.subjectOTUB1
dc.subjectLung cancer
dc.subjectOxidative phosphorylation
dc.subjectMitochondrial proteostasis
dc.title.enThe deubiquitinase OTUB1 governs lung cancer cell fitness by modulating proteostasis of OXPHOS proteins.
dc.title.alternativeBiochim Biophys Acta Mol Basis Disen_US
dc.typeArticle de revueen_US
dc.identifier.doi10.1016/j.bbadis.2023.166767en_US
dc.subject.halSciences du Vivant [q-bio]/Médecine humaine et pathologieen_US
dc.identifier.pubmed37245529en_US
bordeaux.journalBiochimica et Biophysica Acta - Molecular Basis of Diseaseen_US
bordeaux.page166767en_US
bordeaux.volume1869en_US
bordeaux.hal.laboratoriesMaladies Rares : Génétique et Métabolisme (MRGM) - UMR 1211en_US
bordeaux.issue7en_US
bordeaux.institutionUniversité de Bordeauxen_US
bordeaux.institutionINSERMen_US
bordeaux.peerReviewedouien_US
bordeaux.inpressnonen_US
bordeaux.import.sourcepubmed
hal.identifierhal-04312068
hal.version1
hal.date.transferred2023-11-28T13:10:12Z
hal.popularnonen_US
hal.audienceInternationaleen_US
hal.exporttrue
workflow.import.sourcepubmed
dc.rights.ccPas de Licence CCen_US
bordeaux.COinSctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Biochimica%20et%20Biophysica%20Acta%20-%20Molecular%20Basis%20of%20Disease&rft.date=2023-10-01&rft.volume=1869&rft.issue=7&rft.spage=166767&rft.epage=166767&rft.eissn=1879-260X&rft.issn=1879-260X&rft.au=SHERYAZDANOVA,%20Aidana&AMOEDO,%20Nivea%20Dias&DUFOUR,%20Sara&IMPENS,%20Francis&ROSSIGNOL,%20Rodrigue&rft.genre=article


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