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dc.contributor.authorHermann, Clemensen
dc.contributor.authorvan, Hateren Andyen
dc.contributor.authorTrautwein, Nicoen
dc.contributor.authorNeerincx, Andreasen
dc.contributor.authorDuriez, Patrick Jen
dc.contributor.authorStevanović, Stefanen
dc.contributor.authorTrowsdale, Johnen
dc.contributor.authorDeane, Janeten
dc.contributor.authorElliott, Timen
dc.contributor.authorBoyle, Louiseen
dc.date.accessioned2015-10-13T16:10:23Z
dc.date.available2015-10-13T16:10:23Z
dc.date.issued2015-10-06en
dc.identifier.citationHermann et al. eLife (2015) Vol. 4, Article e09617. doi: 10.7554/eLife.09617en
dc.identifier.issn2050-084X
dc.identifier.urihttps://www.repository.cam.ac.uk/handle/1810/251444
dc.description.abstractOur understanding of the antigen presentation pathway has recently been enhanced with the identification that the tapasin-related protein TAPBPR is a second MHC I-specific chaperone. We sought to determine whether, like tapasin, TAPBPR can also influence MHC I peptide selection by functioning as a peptide exchange catalyst. We show that TAPBPR can catalyse the dissociation of peptides from peptide-MHC I complexes, enhance the loading of peptide-receptive MHC I molecules, and discriminate between peptides based on affinity in vitro. In cells, the depletion of TAPBPR increased the diversity of peptides presented on MHC I molecules, suggesting that TAPBPR is involved in restricting peptide presentation. Our results suggest TAPBPR binds to MHC I in a peptide-receptive state and, like tapasin, works to enhance peptide optimisation. It is now clear there are two MHC class I specific peptide editors, tapasin and TAPBPR, intimately involved in controlling peptide presentation to the immune system.
dc.languageEnglishen
dc.language.isoenen
dc.publishereLife
dc.rightsAttribution 2.0 UK: England & Wales*
dc.rights.urihttp://creativecommons.org/licenses/by/2.0/uk/*
dc.titleTAPBPR alters MHC class I peptide presentation by functioning as a peptide exchange catalyst.en
dc.typeArticle
dc.description.versionThis is the final version of the article. It first appeared from eLife via http://dx.doi.org/10.7554en
prism.numbere09617en
prism.publicationDate2015en
prism.publicationNameeLifeen
prism.volume4en
dc.rioxxterms.funderCRUK
dc.rioxxterms.funderRoyal Society
dc.rioxxterms.funderWellcome Trust
dcterms.dateAccepted2015-10-05en
rioxxterms.versionofrecord10.7554/eLife.09617en
rioxxterms.licenseref.urihttp://www.rioxx.net/licenses/all-rights-reserveden
rioxxterms.licenseref.startdate2015-10-06en
dc.contributor.orcidTrowsdale, John [0000-0002-0150-5698]
dc.contributor.orcidDeane, Janet [0000-0002-4863-0330]
dc.contributor.orcidBoyle, Louise [0000-0002-3105-6555]
dc.identifier.eissn2050-084X
rioxxterms.typeJournal Article/Reviewen
pubs.funder-project-idMRC (G0901682)
pubs.funder-project-idWellcome Trust (100140/Z/12/Z)
pubs.funder-project-idWellcome Trust (089821/Z/09/Z)
pubs.funder-project-idWellcome Trust (089563/Z/09/Z)
pubs.funder-project-idWELLCOME TRUST (104647/Z/14/Z)
pubs.funder-project-idRoyal Society (uf100371)
pubs.funder-project-idRoyal Society (1562)
cam.orpheus.successThu Jan 30 12:55:40 GMT 2020 - The item has an open VoR version.*
rioxxterms.freetoread.startdate2300-01-01


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Attribution 2.0 UK: England & Wales
Except where otherwise noted, this item's licence is described as Attribution 2.0 UK: England & Wales