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N-glycosylation of mouse TRAIL-R and human TRAIL-R1 enhances TRAIL-induced death

dc.contributor.authorDUFOUR, Florent
dc.contributor.authorRATTIER, Thibault
dc.contributor.authorSHIRLEY, Sarah
dc.contributor.authorPICARDA, Gaelle
dc.contributor.authorCONSTANTINESCU, Andrei Alexandru
dc.contributor.authorMORLE, Aymeric
dc.contributor.authorZAKARIA, Al Batoul
dc.contributor.authorMARCION, Guillaume
dc.contributor.authorCAUSSE, Sebastien
dc.contributor.authorSZEGEZDI, Eva
dc.contributor.authorZAJONC, Dirk Michael
dc.contributor.authorSEIGNEURIC, Renaud
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorGUICHARD, Gilles
dc.contributor.authorGHARBI, Tijani
dc.contributor.authorPICAUD, Fabien
dc.contributor.authorHERLEM, Guillaume
dc.contributor.authorGARRIDO, Carmen
dc.contributor.authorSCHNEIDER, Pascal
dc.contributor.authorBENEDICT, Chris Alan
dc.contributor.authorMICHEAU, Olivier
dc.date.accessioned2020-07-09T14:16:58Z
dc.date.available2020-07-09T14:16:58Z
dc.date.issued2017-03
dc.identifier.issn1350-9047
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/10330
dc.description.abstractEnAPO2L/TRAIL (TNF-related apoptosis-inducing ligand) induces death of tumor cells through two agonist receptors, TRAIL-R1 and TRAIL-R2. We demonstrate here that N-linked glycosylation (N-glyc) plays also an important regulatory role for TRAIL-R1-mediated and mouse TRAIL receptor (mTRAIL-R)-mediated apoptosis, but not for TRAIL-R2, which is devoid of N-glycans. Cells expressing N-glyc-defective mutants of TRAIL-R1 and mouse TRAIL-R were less sensitive to TRAIL than their wild-type counterparts. Defective apoptotic signaling by N-glyc-deficient TRAIL receptors was associated with lower TRAIL receptor aggregation and reduced DISC formation, but not with reduced TRAIL-binding affinity. Our results also indicate that TRAIL receptor N-glyc impacts immune evasion strategies. The cytomegalovirus (CMV) UL141 protein, which restricts cell-surface expression of human TRAIL death receptors, binds with significant higher affinity TRAIL-R1 lacking N-glyc, suggesting that this sugar modification may have evolved as a counterstrategy to prevent receptor inhibition by UL141. Altogether our findings demonstrate that N-glyc of TRAIL-R1 promotes TRAIL signaling and restricts virus-mediated inhibition.
dc.title.enN-glycosylation of mouse TRAIL-R and human TRAIL-R1 enhances TRAIL-induced death
dc.typeArticle de revue
dc.identifier.doi10.1038/cdd.2016.150
dc.subject.halChimie/Matériaux
bordeaux.journalCell death and differentiation
bordeaux.page500-510
bordeaux.volume24
bordeaux.hal.laboratoriesInstitut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN) - UMR 5248*
bordeaux.hal.laboratoriesInstitut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN, UMR 5248)
bordeaux.issue3
bordeaux.institutionUniversité de Bordeaux
bordeaux.institutionBordeaux INP
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