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dc.contributor.authorDufour, Florent
dc.contributor.authorRattier, Thibault
dc.contributor.authorShirley, Sarah
dc.contributor.authorPicarda, Gaelle
dc.contributor.authorConstantinescu, Andrei Alexandru
dc.contributor.authorMorlé, 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
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.accessioned2018-09-20T16:06:46Z
dc.date.available2018-09-20T16:06:46Z
dc.date.issued2017-02-10
dc.identifier.citationDufour, Florent; Rattier, Thibault; Shirley, Sarah; Picarda, Gaelle; Constantinescu, Andrei Alexandru; Morlé, Aymeric; Zakaria, Al Batoul; Marcion, Guillaume; Causse, Sebastien; Szegezdi, Eva; Zajonc, Dirk Michael; Seigneuric, Renaud; Guichard, Gilles; Gharbi, Tijani; Picaud, Fabien; Herlem, Guillaume; Garrido, Carmen; Schneider, Pascal; Benedict, Chris Alan; Micheau, Olivier (2017). N-glycosylation of mouse trail-r and human trail-r1 enhances trail-induced death. Cell Death and Differentiation 24 (3), 500-510
dc.identifier.issn1350-9047,1476-5403
dc.identifier.urihttp://hdl.handle.net/10379/11286
dc.description.abstractAPO2L/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.publisherSpringer Nature
dc.relation.ispartofCell Death and Differentiation
dc.subjectcancer-cells
dc.subjecthuman cytomegalovirus
dc.subjectcarcinoma cells
dc.subjectreceptor
dc.subjectapoptosis
dc.subjectgalectin-3
dc.subjectapo2l/trail
dc.subjectsialylation
dc.subjectsensitivity
dc.subjectinduction
dc.titleN-glycosylation of mouse trail-r and human trail-r1 enhances trail-induced death
dc.typeArticle
dc.identifier.doi10.1038/cdd.2016.150
dc.local.publishedsourcehttp://www.nature.com/cdd/journal/v24/n3/pdf/cdd2016150a.pdf
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