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dc.rights.licenseopenen_US
dc.contributor.authorTOMAR, Dhanendra
dc.contributor.authorPRAJAPATI, Paresh
hal.structure.identifierUniversité de Bordeaux [UB]
hal.structure.identifierLaboratoire Maladies Rares: Génétique et Métabolisme (Bordeaux) [U1211 INSERM/MRGM]
dc.contributor.authorLAVIE, Julie
dc.contributor.authorSINGH, Kritarth
dc.contributor.authorLAKSHMI, Sripada
dc.contributor.authorBHATELIA, Khyati
dc.contributor.authorROY, Milton
dc.contributor.authorSINGH, Rochika
hal.structure.identifierPhysiopathologie du système nerveux central - Institut François Magendie
hal.structure.identifierUniversité de Bordeaux [UB]
hal.structure.identifierLaboratoire Maladies Rares: Génétique et Métabolisme (Bordeaux) [U1211 INSERM/MRGM]
dc.contributor.authorBENARD, Giovanni
dc.contributor.authorSINGH, Rajesh
dc.date.accessioned2025-02-04T15:23:26Z
dc.date.available2025-02-04T15:23:26Z
dc.date.issued2015-12-01
dc.identifier.issn1873-4596en_US
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/204720
dc.description.abstractEnThe emerging evidences suggest that posttranslational modification of target protein by ubiquitin (Ub) not only regulate its turnover through ubiquitin proteasome system (UPS) but is a critical regulator of various signaling pathways. During ubiquitination, E3 ligase recognizes the target protein and determines the topology of ubiquitin chains. In current study, we studied the role of TRIM4, a member of the TRIM/RBCC protein family of RING E3 ligase, in regulation of hydrogen peroxide (H2O2) induced cell death. TRIM4 is expressed differentially in human tissues and expressed in most of the analyzed human cancer cell lines. The subcellular localization studies showed that TRIM4 forms distinct cytoplasmic speckle like structures which transiently interacts with mitochondria. The expression of TRIM4 induces mitochondrial aggregation and increased level of mitochondrial ROS in the presence of H2O2. It sensitizes the cells to H2O2 induced death whereas knockdown reversed the effect. TRIM4 potentiates the loss of mitochondrial transmembrane potential and cytochrome c release in the presence of H2O2. The analysis of TRIM4 interacting proteins showed its interaction with peroxiredoxin 1 (PRX1), including other proteins involved in regulation of mitochondrial and redox homeostasis. TRIM4 interaction with PRX1 is critical for the regulation of H2O2 induced cell death. Collectively, the evidences in the current study suggest the role of TRIM4 in regulation of oxidative stress induced cell death.
dc.language.isoENen_US
dc.subject.enCell death
dc.subject.enH(2)O(2)
dc.subject.enMitochondria
dc.subject.enPRX1
dc.subject.enTRIM4
dc.subject.enUbiquitin E3 ligase
dc.title.enTRIM4; a novel mitochondrial interacting RING E3 ligase, sensitizes the cells to hydrogen peroxide (H2O2) induced cell death.
dc.title.alternativeFree Radic Biol Meden_US
dc.typeArticle de revueen_US
dc.identifier.doi10.1016/j.freeradbiomed.2015.10.425en_US
dc.subject.halSciences du Vivant [q-bio]/Génétiqueen_US
dc.identifier.pubmed26524401en_US
bordeaux.journalFree Radical Biology and Medicineen_US
bordeaux.page1036-48en_US
bordeaux.volume89en_US
bordeaux.hal.laboratoriesMaladies Rares : Génétique et Métabolisme (MRGM) - UMR 1211en_US
bordeaux.institutionUniversité de Bordeauxen_US
bordeaux.institutionINSERMen_US
bordeaux.peerReviewedouien_US
bordeaux.inpressnonen_US
bordeaux.import.sourcepubmed
hal.identifierhal-04929303
hal.version1
hal.date.transferred2025-02-04T15:23:29Z
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=Free%20Radical%20Biology%20and%20Medicine&rft.date=2015-12-01&rft.volume=89&rft.spage=1036-48&rft.epage=1036-48&rft.eissn=1873-4596&rft.issn=1873-4596&rft.au=TOMAR,%20Dhanendra&PRAJAPATI,%20Paresh&LAVIE,%20Julie&SINGH,%20Kritarth&LAKSHMI,%20Sripada&rft.genre=article


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