Glycoprotein folding and the role of EDEM1, EDEM2 and EDEM3 in degradation of folding-defective glycoproteins

被引：107

作者：

Olivari, Silvia ^{[1
]}

Molinari, Maurizio ^{[1
]}

机构：

[1] Biomed Res Inst, CH-6500 Bellinzona, Switzerland

来源：

FEBS LETTERS | 2007年 / 581卷 / 19期

关键词：

endoplasmic reticulum; protein folding; ER-associated degradation (ERAD); EDEM1; EDEM2; EDEM3; RETICULUM-ASSOCIATED DEGRADATION; MANNOSIDASE-LIKE PROTEIN; ER-ASSOCIATED DEGRADATION; SHORT-LIVED VARIANT; ENDOPLASMIC-RETICULUM; MISFOLDED GLYCOPROTEINS; QUALITY-CONTROL; N-GLYCAN; SACCHAROMYCES-CEREVISIAE; CALNEXIN;

D O I：

10.1016/j.febslet.2007.04.070

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：

Proteins synthesized in the endoplasmic reticulurn (ER) lumen are exposed to several dedicated chaperones and folding factors that ensure efficient maturation. Nevertheless, protein folding remains error-prone and mutations in the polypeptide sequence may significantly reduce folding-efficiency. Folding-incompetent proteins carrying N-glycans are extracted from futile folding cycles in the calnexin chaperone system upon intervention of EDEM1, EDEM2 and EDEM3, three ER-stress-induced members of the glycosyl hydrolase 47 family. This review describes current knowledge about mechanisms regulating folding and disposal of glycoproteins. (c) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

收藏

页码：3658 / 3664

页数：7

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