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Non-phosphorylatable mutants of Ser184 lead to incomplete activation of Bax

dc.rights.licenseopenen_US
hal.structure.identifierInstitut de biochimie et génétique cellulaires [IBGC]
dc.contributor.authorSIMONYAN, Lilit
hal.structure.identifierInstitut de biochimie et génétique cellulaires [IBGC]
dc.contributor.authorGONIN, Mathilde
dc.contributor.authorHANKS, James
dc.contributor.authorFRIEDLEIN, Jordan
hal.structure.identifierInstitut de biochimie et génétique cellulaires [IBGC]
dc.contributor.authorDUTREC, Kevin
hal.structure.identifierInstitut de biochimie et génétique cellulaires [IBGC]
dc.contributor.authorAROKIUM, Hubert
hal.structure.identifierInstitut de biochimie et génétique cellulaires [IBGC]
dc.contributor.authorROUCHIDANE EYITAYO, Akande
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorDOUDY, Toukounou Megann
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorCHAIGNEPAIN, Stephane
hal.structure.identifierInstitut de biochimie et génétique cellulaires [IBGC]
dc.contributor.authorMANON, Stephen
dc.contributor.authorDEJEAN, Laurent
dc.date.accessioned2024-04-30T12:48:44Z
dc.date.available2024-04-30T12:48:44Z
dc.date.issued2023
dc.identifier.issn2234-943Xen_US
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/199546
dc.description.abstractEnThe S184 residue of Bax is the target of several protein kinases regulating cell fate, including AKT. It is well-established that, in cellulo , the substitution of S184 by a non-phosphorylatable residue stimulates both the mitochondrial localization of Bax, cytochrome c release, and apoptosis. However, in in vitro experiments, substituted mutants did not exhibit any increase in their binding capacity to isolated mitochondria or liposomes. Despite exhibiting a significant increase of the 6A7 epitope exposure, substituted mutants remain limited in their ability to form large oligomers, suggesting that they high capacity to promote apoptosis in cells was more related to a high content than to an increased ability to form large pores in the outer mitochondrial membranes.
dc.language.isoENen_US
dc.title.enNon-phosphorylatable mutants of Ser184 lead to incomplete activation of Bax
dc.typeArticle de revueen_US
dc.identifier.doi10.3389/fonc.2022.1068994en_US
dc.subject.halSciences du Vivant [q-bio]/Biologie cellulaire/Organisation et fonctions cellulaires [q-bio.SC]en_US
dc.subject.halSciences du Vivant [q-bio]/Biochimie, Biologie Moléculaireen_US
bordeaux.journalFrontiers in Oncologyen_US
bordeaux.volume12en_US
bordeaux.hal.laboratoriesCBMN : Chimie & de Biologie des Membranes & des Nano-objets - UMR 5248en_US
bordeaux.institutionUniversité de Bordeauxen_US
bordeaux.institutionBordeaux INPen_US
bordeaux.institutionCNRSen_US
bordeaux.peerReviewedouien_US
bordeaux.inpressnonen_US
bordeaux.import.sourcehal
hal.identifierhal-04255643
hal.version1
hal.popularnonen_US
hal.audienceInternationaleen_US
hal.exportfalse
workflow.import.sourcehal
dc.rights.ccPas de Licence CCen_US
bordeaux.COinSctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Frontiers%20in%20Oncology&rft.date=2023&rft.volume=12&rft.eissn=2234-943X&rft.issn=2234-943X&rft.au=SIMONYAN,%20Lilit&GONIN,%20Mathilde&HANKS,%20James&FRIEDLEIN,%20Jordan&DUTREC,%20Kevin&rft.genre=article


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