Lectins as chaperones in glycoprotein folding

被引：200

作者：

Trombetta, ES

Helenius, A

机构：

[1] Yale Univ, Sch Med, Dept Cell Biol, New Haven, CT 06520 USA

[2] Swiss Fed Inst Technol, Dept Biochem, CH-8092 Zurich, Switzerland

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 1998年 / 8卷 / 05期

关键词：

D O I：

10.1016/S0959-440X(98)80148-6

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：

N-glycosylation allows newly synthesized glycoproteins to interact with a lectin-based chaperone system in the endoplasmic reticulum. Binding to the lectins calnexin and calreticulin is mediated by monoglucosylated oligosaccharides that are produced transiently by the deglucosylation and reglucosylation of substrate glycoproteins during their maturation process. In mammalian cells, calnexin, calreticulin and associated factors promote the correct folding and oligomerization of many glycoproteins, providing unique quality control and chaperone functions specific for glycoproteins in the endoplasmic reticulum.

引用

页码：587 / 592

页数：6

共 48 条

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