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

TAPBPR bridges UDP-glucose: glycoprotein glucosyltransferase 1 onto MHC class I to provide quality control in the antigen presentation pathway
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 that is important for optimal peptide selection by MHC class I molecules. Here, we asked whether 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 that is 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 MHC class I molecules. We reveal that the interaction between TAPBPR and UGT1 facilities the reglucosylation of the glycan on MHC class I molecules, 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.
2050-084X
1-25
Neerincx, Andreas
e487d7b5-1d13-4847-83b2-67fc2754c238
Hermann, Clemens
978cedee-4017-43e9-86a7-4665636ce553
Antrobus, Robin
75b80a44-cef2-4f9c-8e5d-a0dba18a9868
Van Hateren, Andrew
e345fa3c-d89c-4b91-947e-c1d818cc7f71
Cao, Huan
7b63147f-6ab7-4348-8d0a-a9ff5fd6cf64
Trautwein, Nico
2387bf8d-9384-4edb-93e7-3cefe5021ae7
Stevanović, Stefan
e09af639-b73f-459b-b111-55a6c722b03d
Elliott, Tim
16670fa8-c2f9-477a-91df-7c9e5b453e0e
Deane, Janet E.
dd93a448-fe81-4c8b-884e-a396ada0cebd
Boyle, Louise H.
e2afc84e-3524-417d-a54b-4f7f7d753866
Neerincx, Andreas
e487d7b5-1d13-4847-83b2-67fc2754c238
Hermann, Clemens
978cedee-4017-43e9-86a7-4665636ce553
Antrobus, Robin
75b80a44-cef2-4f9c-8e5d-a0dba18a9868
Van Hateren, Andrew
e345fa3c-d89c-4b91-947e-c1d818cc7f71
Cao, Huan
7b63147f-6ab7-4348-8d0a-a9ff5fd6cf64
Trautwein, Nico
2387bf8d-9384-4edb-93e7-3cefe5021ae7
Stevanović, Stefan
e09af639-b73f-459b-b111-55a6c722b03d
Elliott, Tim
16670fa8-c2f9-477a-91df-7c9e5b453e0e
Deane, Janet E.
dd93a448-fe81-4c8b-884e-a396ada0cebd
Boyle, Louise H.
e2afc84e-3524-417d-a54b-4f7f7d753866

Neerincx, Andreas, Hermann, Clemens, Antrobus, Robin, Van Hateren, Andrew, Cao, Huan, Trautwein, Nico, Stevanović, Stefan, Elliott, Tim, Deane, Janet E. and Boyle, Louise H. (2017) TAPBPR bridges UDP-glucose: glycoprotein glucosyltransferase 1 onto MHC class I to provide quality control in the antigen presentation pathway. eLife, 2017 (6), 1-25, [e23049]. (doi:10.7554/eLife.23049.001).

Record type: Article

Abstract

Recently, we revealed that TAPBPR is a peptide exchange catalyst that is important for optimal peptide selection by MHC class I molecules. Here, we asked whether 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 that is 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 MHC class I molecules. We reveal that the interaction between TAPBPR and UGT1 facilities the reglucosylation of the glycan on MHC class I molecules, 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.

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elife-23049-v2 - Version of Record
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Accepted/In Press date: 14 April 2017
e-pub ahead of print date: 20 April 2017
Published date: 23 May 2017

Identifiers

Local EPrints ID: 412751
URI: http://eprints.soton.ac.uk/id/eprint/412751
ISSN: 2050-084X
PURE UUID: f0cbbf34-2bd9-425d-b472-afcbe5d2d5e9
ORCID for Andrew Van Hateren: ORCID iD orcid.org/0000-0002-3915-0239
ORCID for Tim Elliott: ORCID iD orcid.org/0000-0003-1097-0222

Catalogue record

Date deposited: 31 Jul 2017 16:31
Last modified: 22 Nov 2021 02:54

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Contributors

Author: Andreas Neerincx
Author: Clemens Hermann
Author: Robin Antrobus
Author: Huan Cao
Author: Nico Trautwein
Author: Stefan Stevanović
Author: Tim Elliott ORCID iD
Author: Janet E. Deane
Author: Louise H. Boyle

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