Glycoprotein folding in the endoplasmic reticulum: a tale of three chaperones?

被引：125

作者：

High, S ^{[1
]}

Lecomte, FJL ^{[1
]}

Russell, SJ ^{[1
]}

Abell, BM ^{[1
]}

Oliver, JD ^{[1
]}

机构：

[1] Univ Manchester, Sch Biol Sci, Manchester M13 9PT, Lancs, England

来源：

FEBS LETTERS | 2000年 / 476卷 / 1-2期

关键词：

endoplasmic reticulum; glycoprotein; protein folding; molecular chaperone; calnexin; ERp57;

D O I：

10.1016/S0014-5793(00)01666-5

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：

The endoplasmic reticulum (ER) is a major site of protein synthesis and its inside, or lumen, is a major site of protein folding, The lumen of the ER contains many folding factors and molecular chaperones, which facilitate protein folding by increasing both the rate and the efficiency of this process. Amongst the many ER folding factors, there are three components that specifically modulate the folding glycoproteins bearing N-linked carbohydrate side chains. These components are calnexin, calreticulin and ERp57, and this review focuses on the molecular basis for their capacity to influence glycoprotein folding. (C) 2000 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.

引用

页码：38 / 41

页数：4