Properties of the tapasin homologue TAPBPR
Accepted version
Peer-reviewed
Repository URI
Repository DOI
Change log
Authors
Neerincx, A
Boyle, LH
Abstract
The presentation of antigenic peptides by MHC class I molecules plays a vital role in generating T cell responses against infection and cancer. Over the last two decades the central role of tapasin as a peptide editor that influences the loading and optimisation of peptides onto MHC class I molecules has been extensively characterised. Recently, it has become evident that the tapasin-related protein, TAPBPR, functions as a second peptide editor which influences the peptides displayed by MHC class I molecules. Here, we review the discovery of TAPBPR and current understanding of this novel protein in relation to its closest homologue tapasin.
Description
Keywords
Animals, Antigen Presentation, Cellular Microenvironment, Epitopes, Histocompatibility Antigens Class I, Humans, Immunoglobulins, Membrane Proteins, Membrane Transport Proteins, Molecular Chaperones, Peptides, Polymorphism, Genetic, Protein Binding, Protein Isoforms, Signal Transduction, T-Lymphocyte Subsets
Journal Title
Current Opinion in Immunology
Conference Name
Journal ISSN
0952-7915
1879-0372
1879-0372
Volume Title
46
Publisher
Elsevier BV
Publisher DOI
Sponsorship
Wellcome Trust (085038/Z/08/Z)
Wellcome Trust (104647/Z/14/Z)
Wellcome Trust (104647/Z/14/Z)
This work was funded by a Wellcome Trust Senior Research Fellowship 104647/Z/14/Z.