Chaperones and folding of MHC class I molecules in the endoplasmic reticulum

被引:55
作者
Paulsson, K
Wang, P
机构
[1] Lund Univ, Inst Tumour Immunol, S-22362 Lund, Sweden
[2] London Sch Med & Dent, Dept Gastroenterol, Immunol Grp, London EC1A 7ED, England
来源
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH | 2003年 / 1641卷 / 01期
关键词
endoplasmic reticulum (ER); MEC class I; folding; chaperone; tapasin;
D O I
10.1016/S0167-4889(03)00048-X
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
In this review we discuss the influence of chaperones on the general phenomena of folding as well as on the specific folding of an individual protein, MHC class I. MHC class I maturation is a highly sophisticated process in which the folding machinery of the endoplasmic reticulum (ER) is heavily involved. Understanding the MHC class I maturation per se is important since peptides loaded onto MHC class I molecules are the base for antigen presentation generating immune responses against virus, intracellular bacteria as well as tumours. This review discusses the early stages of MHC class I maturation regarding BiP and calnexin association, and differences in MHC class I heavy chain (HC) interaction with calnexin and calreticulin are highlighted. Late stage MHC class I maturation with focus on the dedicated chaperone tapasin is also discussed. (C) 2003 Elsevier Science B.V. All rights reserved.
引用
收藏
页码:1 / 12
页数:12
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