Intracellular surveillance: Controlling the assembly of MHC class I-peptide complexes

被引：57

作者：

Cresswell, P ^{[1
]}

机构：

[1] Yale Univ, Sch Med, Howard Hughes Med Inst, New Haven, CT 06510 USA

来源：

TRAFFIC | 2000年 / 1卷 / 04期

关键词：

calnexin; calreticulin; chaperone; ERp57; HLA; MHC; TAP; tapasin;

D O I：

10.1034/j.1600-0854.2000.010402.x

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

MHC class I molecules bind with high affinity to peptides in the endoplasmic reticulum and display them on the cell surface. Here they are screened by CD8-positive T-lymphocytes for the presence of foreign, pathogen-derived peptides within the mass of self-peptides expressed. MHC class I assembly is a complicated process involving a number of accessory molecules, including specialized components as well as common chaperones. Our understanding of the mechanisms involved, while quite advanced, is far from complete.

引用

页码：301 / 305

页数：5

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