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TAPBPR isoforms exhibit altered association with MHC class I

The tapasin-related protein TAPBPR is a novel component of the antigen processing and presentation pathway, which binds to MHC class I coupled with β(2)-microglobulin. We describe six alternatively spliced TAPBPR transcripts from the TAPBPL gene and investigate three of these at a protein level. TAP...

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Detalles Bibliográficos
Autores principales: Porter, Keith M, Hermann, Clemens, Traherne, James A, Boyle, Louise H
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley & Sons Ltd 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4008236/
https://www.ncbi.nlm.nih.gov/pubmed/24444341
http://dx.doi.org/10.1111/imm.12253
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author Porter, Keith M
Hermann, Clemens
Traherne, James A
Boyle, Louise H
author_facet Porter, Keith M
Hermann, Clemens
Traherne, James A
Boyle, Louise H
author_sort Porter, Keith M
collection PubMed
description The tapasin-related protein TAPBPR is a novel component of the antigen processing and presentation pathway, which binds to MHC class I coupled with β(2)-microglobulin. We describe six alternatively spliced TAPBPR transcripts from the TAPBPL gene and investigate three of these at a protein level. TAPBPR transcripts lacking exon 5 result in loss of the membrane proximal IgC domain and loss of ability to bind to MHC class I. Alternative acceptor and donor splice sites in exon 4 of TAPBPR altered the reading frame in the IgV domain and produced a truncated TAPBPR product. An additional exon in the TAPBPL gene was identified that encodes extra residues in the cytoplasmic tail of TAPBPR. This longer TAPBPR protein interacted with MHC class I but was attenuated in its ability to down-regulate surface expression of MHC class I. The abundance of these alternative transcripts in peripheral blood mononuclear cells and dendritic cells suggests an important role of TAPBPR isoforms in vivo.
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spelling pubmed-40082362014-12-03 TAPBPR isoforms exhibit altered association with MHC class I Porter, Keith M Hermann, Clemens Traherne, James A Boyle, Louise H Immunology Research Articles The tapasin-related protein TAPBPR is a novel component of the antigen processing and presentation pathway, which binds to MHC class I coupled with β(2)-microglobulin. We describe six alternatively spliced TAPBPR transcripts from the TAPBPL gene and investigate three of these at a protein level. TAPBPR transcripts lacking exon 5 result in loss of the membrane proximal IgC domain and loss of ability to bind to MHC class I. Alternative acceptor and donor splice sites in exon 4 of TAPBPR altered the reading frame in the IgV domain and produced a truncated TAPBPR product. An additional exon in the TAPBPL gene was identified that encodes extra residues in the cytoplasmic tail of TAPBPR. This longer TAPBPR protein interacted with MHC class I but was attenuated in its ability to down-regulate surface expression of MHC class I. The abundance of these alternative transcripts in peripheral blood mononuclear cells and dendritic cells suggests an important role of TAPBPR isoforms in vivo. John Wiley & Sons Ltd 2014-06 2014-04-24 /pmc/articles/PMC4008236/ /pubmed/24444341 http://dx.doi.org/10.1111/imm.12253 Text en © 2014 The Authors. Immunology published by John Wiley & Sons Ltd. Immunology, http://creativecommons.org/licenses/by/3.0/ This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Articles
Porter, Keith M
Hermann, Clemens
Traherne, James A
Boyle, Louise H
TAPBPR isoforms exhibit altered association with MHC class I
title TAPBPR isoforms exhibit altered association with MHC class I
title_full TAPBPR isoforms exhibit altered association with MHC class I
title_fullStr TAPBPR isoforms exhibit altered association with MHC class I
title_full_unstemmed TAPBPR isoforms exhibit altered association with MHC class I
title_short TAPBPR isoforms exhibit altered association with MHC class I
title_sort tapbpr isoforms exhibit altered association with mhc class i
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4008236/
https://www.ncbi.nlm.nih.gov/pubmed/24444341
http://dx.doi.org/10.1111/imm.12253
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