期刊
ANNUAL REVIEW OF CELL AND DEVELOPMENTAL BIOLOGY
卷 24, 期 -, 页码 343-368出版社
ANNUAL REVIEWS
DOI: 10.1146/annurev.cellbio.24.110707.175347
关键词
tapasin; ERp57; glycoprotein folding; antigen processing
资金
- Howard Hughes Medical Institute (P.C.)
- NIH/National Institute of General Medical Sciences Medical Scientist Training Grant [GM07205]
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [T32GM007205] Funding Source: NIH RePORTER
Peptide binding to MHC class I molecules is a component of a folding and assembly, process that occurs in the endoplasmic reticulum (ER) and uses both cellular chaperones and dedicated factors. The involvement of glycoprotein quality-control chaperones and cellular oxidoreductases in peptide binding has led to models that are gradually being refined. Some aspects of the peptide loading process (e.g., the biosynthesis and degradation of MHC class I complexes) conform to models of glycoprotein quality control, but other aspects (e.g., the formation of a stable disulfide-linked dimer between tapasin and ERp57) deviate from models of chaperone and oxidoreductase function. Here we review what is known about the intersection of glycoprotein folding, oxidative reactions, and MHC class I peptide loading, emphasizing events that occur in the ER and within the MHC class I peptide loading complex.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据