The University of Southampton
University of Southampton Institutional Repository
Warning ePrints Soton is experiencing an issue with some file downloads not being available. We are working hard to fix this. Please bear with us.

Data from: TAPBPR bridges UDP-glucose:glycoprotein glucosyltransferase 1 onto MHC class I to provide quality control in the antigen presentation pathway

Data from: TAPBPR bridges UDP-glucose:glycoprotein glucosyltransferase 1 onto MHC class I to provide quality control in the antigen presentation pathway
Data from: TAPBPR bridges UDP-glucose:glycoprotein glucosyltransferase 1 onto MHC class I to provide quality control in the antigen presentation pathway
Recently we revealed that TAPBPR is a peptide exchange catalyst important for optimal peptide selection by MHC class I molecules. Here we asked if any other co-factors associate with TAPBPR which would explain its effect on peptide selection. We identify an interaction between TAPBPR and UDP-glucose:glycoprotein glucosyltransferase 1 (UGT1), a folding sensor in the calnexin/calreticulin quality control cycle known to regenerate the Glc1Man9GlcNAc2 moiety on glycoproteins. Our results suggest the formation of a multimeric complex, dependent on a conserved cysteine at position 94 in TAPBPR, in which TAPBPR promotes the association of UGT1 with peptide-receptive class I molecules. We reveal that the interaction between TAPBPR and UGT1 facilities the reglucosylation of the glycan on class I, promoting their recognition by calreticulin. Our results suggest that in addition to being a peptide-editor, TAPBPR improves peptide optimisation by promoting peptide-receptive MHC class I molecules to associate with the peptide-loading complex.,MHC I peptide elutions from TAPBPR-WT and TAPBPR-C94A expressing cellsPeptide list version 2.xlsx,
DRYAD
Neerincx, Andreas
e487d7b5-1d13-4847-83b2-67fc2754c238
Hermann, Clemens
978cedee-4017-43e9-86a7-4665636ce553
Antrobus, Robin
75b80a44-cef2-4f9c-8e5d-a0dba18a9868
Van Hateren, Andy
e345fa3c-d89c-4b91-947e-c1d818cc7f71
Huan, Cao
Trautwein, Nico
2387bf8d-9384-4edb-93e7-3cefe5021ae7
Stevanović, Stefan
e09af639-b73f-459b-b111-55a6c722b03d
Elliott, Timothy
16670fa8-c2f9-477a-91df-7c9e5b453e0e
Deane, Janet E.
dd93a448-fe81-4c8b-884e-a396ada0cebd
Boyle, Louise H.
e2afc84e-3524-417d-a54b-4f7f7d753866
Cao, Huan
7b63147f-6ab7-4348-8d0a-a9ff5fd6cf64
Neerincx, Andreas
e487d7b5-1d13-4847-83b2-67fc2754c238
Hermann, Clemens
978cedee-4017-43e9-86a7-4665636ce553
Antrobus, Robin
75b80a44-cef2-4f9c-8e5d-a0dba18a9868
Van Hateren, Andy
e345fa3c-d89c-4b91-947e-c1d818cc7f71
Huan, Cao
Trautwein, Nico
2387bf8d-9384-4edb-93e7-3cefe5021ae7
Stevanović, Stefan
e09af639-b73f-459b-b111-55a6c722b03d
Elliott, Timothy
16670fa8-c2f9-477a-91df-7c9e5b453e0e
Deane, Janet E.
dd93a448-fe81-4c8b-884e-a396ada0cebd
Boyle, Louise H.
e2afc84e-3524-417d-a54b-4f7f7d753866
Cao, Huan
7b63147f-6ab7-4348-8d0a-a9ff5fd6cf64

Neerincx, Andreas, Hermann, Clemens, Antrobus, Robin, Trautwein, Nico, Stevanović, Stefan, Elliott, Timothy, Deane, Janet E., Boyle, Louise H. and Cao, Huan (2018) Data from: TAPBPR bridges UDP-glucose:glycoprotein glucosyltransferase 1 onto MHC class I to provide quality control in the antigen presentation pathway. DRYAD doi:10.5061/dryad.8fh3g [Dataset]

Record type: Dataset

Abstract

Recently we revealed that TAPBPR is a peptide exchange catalyst important for optimal peptide selection by MHC class I molecules. Here we asked if any other co-factors associate with TAPBPR which would explain its effect on peptide selection. We identify an interaction between TAPBPR and UDP-glucose:glycoprotein glucosyltransferase 1 (UGT1), a folding sensor in the calnexin/calreticulin quality control cycle known to regenerate the Glc1Man9GlcNAc2 moiety on glycoproteins. Our results suggest the formation of a multimeric complex, dependent on a conserved cysteine at position 94 in TAPBPR, in which TAPBPR promotes the association of UGT1 with peptide-receptive class I molecules. We reveal that the interaction between TAPBPR and UGT1 facilities the reglucosylation of the glycan on class I, promoting their recognition by calreticulin. Our results suggest that in addition to being a peptide-editor, TAPBPR improves peptide optimisation by promoting peptide-receptive MHC class I molecules to associate with the peptide-loading complex.,MHC I peptide elutions from TAPBPR-WT and TAPBPR-C94A expressing cellsPeptide list version 2.xlsx,

This record has no associated files available for download.

More information

Published date: 1 January 2018

Identifiers

Local EPrints ID: 448684
URI: http://eprints.soton.ac.uk/id/eprint/448684
PURE UUID: 581390fa-50e7-4ab7-abaf-3ee21bb36158
ORCID for Andy Van Hateren: ORCID iD orcid.org/0000-0002-3915-0239
ORCID for Timothy Elliott: ORCID iD orcid.org/0000-0003-1097-0222

Catalogue record

Date deposited: 29 Apr 2021 16:32
Last modified: 30 Apr 2021 01:40

Export record

Altmetrics

Contributors

Creator: Andreas Neerincx
Creator: Clemens Hermann
Creator: Robin Antrobus
Contributor: Andy Van Hateren ORCID iD
Contributor: Cao Huan
Creator: Nico Trautwein
Creator: Stefan Stevanović
Creator: Timothy Elliott ORCID iD
Creator: Janet E. Deane
Creator: Louise H. Boyle
Creator: Huan Cao

Download statistics

Downloads from ePrints over the past year. Other digital versions may also be available to download e.g. from the publisher's website.

View more statistics

Atom RSS 1.0 RSS 2.0

Contact ePrints Soton: eprints@soton.ac.uk

ePrints Soton supports OAI 2.0 with a base URL of http://eprints.soton.ac.uk/cgi/oai2

This repository has been built using EPrints software, developed at the University of Southampton, but available to everyone to use.

We use cookies to ensure that we give you the best experience on our website. If you continue without changing your settings, we will assume that you are happy to receive cookies on the University of Southampton website.

×