Hermann C, Trowsdale J, Boyle L H
Department of Pathology, University of Cambridge, Cambridge CB2 1QP, UK.
Tissue Antigens. 2015 Mar;85(3):155-66. doi: 10.1111/tan.12538.
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.
为了使T细胞对病原体和肿瘤产生特异性反应,主要组织相容性复合体(MHC)I类分子在细胞表面向T细胞呈递高亲和力肽段。肽段装载的一个关键参与者是MHC I类专用伴侣蛋白塔帕辛。最近,我们发现了第二种MHC I类专用伴侣蛋白,即塔帕辛相关蛋白TAPBPR。在此,我们回顾了MHC I类途径中的主要步骤以及TAPBPR的数据。我们讨论了TAPBPR在MHC I类途径中的潜在功能,以及这种以前未被表征的蛋白质在人类健康和疾病中的作用。