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TAPBPR: a new player in the MHC class I presentation pathway.


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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

Journal Title

Tissue Antigens

Conference Name

Journal ISSN

2059-2302
1399-0039

Volume Title

85

Publisher

Wiley

Rights and licensing

Except where otherwised noted, this item's license is described as All rights reserved
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)
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).