| Literature DB >> 25720504 |
C Hermann1, J Trowsdale, L H Boyle.
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.Entities:
Keywords: TAPBPR/TAPBPL; antigen processing and presentation; disease association; human; major histocompatibility complex (MHC); tapasin
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Year: 2015 PMID: 25720504 DOI: 10.1111/tan.12538
Source DB: PubMed Journal: Tissue Antigens ISSN: 0001-2815