TAPBPR: a new player in the MHC class I presentation pathway.
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Authors
Abstract
In order to provide specificity for T cell responses against pathogens and tumours, major histocompatibility complex (MHC) class I molecules present high-affinity peptides at the cell surface to T cells. A key player for peptide loading is the MHC class I-dedicated chaperone tapasin. Recently we discovered a second MHC class I-dedicated chaperone, the tapasin-related protein TAPBPR. Here, we review the major steps in the MHC class I pathway and the TAPBPR data. We discuss the potential function of TAPBPR in the MHC class I pathway and the involvement of this previously uncharacterised protein in human health and disease.
Description
Keywords
TAPBPR/TAPBPL, antigen processing and presentation, disease association, human, major histocompatibility complex (MHC), tapasin, Amino Acid Sequence, Antigen Presentation, Antigen-Presenting Cells, Cell Membrane, Endoplasmic Reticulum, Gene Expression, Histocompatibility Antigens Class I, Humans, Immunoglobulins, Membrane Proteins, Membrane Transport Proteins, Models, Molecular, Molecular Sequence Data, Peptides, Protein Transport, Signal Transduction
Journal Title
Tissue Antigens
Conference Name
Journal ISSN
0001-2815
1399-0039
1399-0039
Volume Title
85
Publisher
Wiley
Publisher DOI
Sponsorship
Wellcome Trust (100140/Z/12/Z)
Wellcome Trust (104647/Z/14/Z)
Wellcome Trust (085038/Z/08/Z)
Wellcome Trust (089563/Z/09/Z)
Wellcome Trust (104647/Z/14/Z)
Wellcome Trust (085038/Z/08/Z)
Wellcome Trust (089563/Z/09/Z)
C.H was supported by a Wellcome Trust PhD Studentship (Grant 089563) and L.H.B was
funded by a Wellcome Trust Career Development Fellowship (Grant 085038).