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dc.rights.licenseopenen_US
dc.contributor.authorAL ABYAD, Dina
dc.contributor.authorSERFATY, Xavier
hal.structure.identifierUniversité de Bordeaux [UB]
dc.contributor.authorLEFRANÇOIS, Pauline
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorARBAULT, Stephane
dc.contributor.authorBACIOU, Laura
dc.contributor.authorDUPRE-CROCHET, Sophie
dc.contributor.authorKOUZAYHA, Achraf
dc.contributor.authorBIZOUARN, Tania
dc.date.accessioned2024-04-30T10:36:08Z
dc.date.available2024-04-30T10:36:08Z
dc.date.issued2023
dc.identifier.issn0005-2736en_US
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/199533
dc.description.abstractEnIn phagocytes, superoxide anion (O2 •-), the precursor of reactive oxygen species, is produced by the NADPH oxidase complex to kill pathogens. Phagocyte NADPH oxidase consists of the transmembrane cytochrome b558 (cyt b558) and four cytosolic components: p40 phox , p47 phox , p67 phox , and Rac1/2. The phagocyte activation by stimuli leads to activation of signal transduction pathways. This is followed by the translocation of cytosolic components to the membrane and their association with cyt b558 to form the active enzyme. To investigate the roles of membrane-interacting domains of the cytosolic proteins in the NADPH oxidase complex assembly and activity, we used giant unilamellar phospholipid vesicles (GUV). We also used the neutrophil-like cell line PLB-985 to investigate these roles under physiological conditions. We confirmed that the isolated proteins must be activated to bind to the membrane. We showed that their membrane binding was strengthened by the presence of the other cytosolic partners, with a key role for p47 phox. We also used a fused chimera consisting of p47 phox (aa 1-286), p67 phox (aa 1-212) and Rac1Q61L, as well as mutated versions in the p47 phox PX domain and the Rac polybasic region (PB). We showed that these two domains have a crucial role in the trimera membrane-binding and in the trimera assembly to cyt b558. They also have an impact on O2.-production in vitro and in cellulo: the PX domain strongly binding to GUV made of a mix of polar lipids; and the PB region strongly binding to the plasma membrane of neutrophils and resting PLB-985 cells.
dc.description.sponsorshipIdex Paris-Saclay - ANR-11-IDEX-0003en_US
dc.language.isoENen_US
dc.subject.enNADPH oxidase
dc.subject.enphagocyte
dc.subject.enPLB-985
dc.subject.enlipid-protein interaction
dc.subject.enGUV
dc.subject.enprotein complex assembly
dc.title.enRole of the phospholipid binding sites, PX of p47 phox and PB region of Rac1, in the formation of the phagocyte NADPH oxidase complex NOX2
dc.typeArticle de revueen_US
dc.identifier.doi10.1016/j.bbamem.2023.184180en_US
dc.subject.halSciences du Vivant [q-bio]/Biochimie, Biologie Moléculaireen_US
bordeaux.journalBiochimica et Biophysica Acta:Biomembranesen_US
bordeaux.page184180en_US
bordeaux.volume1865en_US
bordeaux.hal.laboratoriesCBMN : Chimie & de Biologie des Membranes & des Nano-objets - UMR 5248en_US
bordeaux.issue7en_US
bordeaux.institutionUniversité de Bordeauxen_US
bordeaux.institutionBordeaux INPen_US
bordeaux.institutionCNRSen_US
bordeaux.peerReviewedouien_US
bordeaux.inpressnonen_US
bordeaux.import.sourcehal
hal.identifierhal-04129544
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=Biochimica%20et%20Biophysica%20Acta:Biomembranes&rft.date=2023&rft.volume=1865&rft.issue=7&rft.spage=184180&rft.epage=184180&rft.eissn=0005-2736&rft.issn=0005-2736&rft.au=AL%20ABYAD,%20Dina&SERFATY,%20Xavier&LEFRAN%C3%87OIS,%20Pauline&ARBAULT,%20Stephane&BACIOU,%20Laura&rft.genre=article


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