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

被引：21

作者：

Hermann, C. ^{[1
]}

Trowsdale, J. ^{[1
]}

Boyle, L. H. ^{[1
]}

机构：

[1] Univ Cambridge, Dept Pathol, Cambridge CB2 1QP, England

来源：

TISSUE ANTIGENS | 2015年 / 85卷 / 03期

基金：

英国惠康基金;

关键词：

antigen processing and presentation; disease association; human; major histocompatibility complex (MHC); tapasin; TAPBPR; TAPBPL; HLA CLASS-I; PEPTIDE-LOADING COMPLEX; INDEPENDENT PROCESSING PATHWAYS; INVARIANT CHAIN ASSOCIATION; CALRETICULIN P-DOMAIN; ENDOPLASMIC-RETICULUM; ANTIGEN PRESENTATION; QUALITY-CONTROL; ANKYLOSING-SPONDYLITIS; DR MOLECULES;

D O I：

10.1111/tan.12538

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

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.

引用

页码：155 / 166

页数：12

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