Cotranslational and posttranslocational N-glycosylation of proteins in the endoplasmic reticulum

被引：118

作者：

Shrimal, Shiteshu ^{[1
]}

Cherepanova, Natalia A. ^{[1
]}

Gilmore, Reid ^{[1
]}

机构：

[1] Univ Massachusetts, Sch Med, Dept Biochem & Mol Pharmacol, Worcester, MA 01605 USA

来源：

SEMINARS IN CELL & DEVELOPMENTAL BIOLOGY | 2015年 / 41卷

基金：

美国国家卫生研究院;

关键词：

Asparagine linked glycosylation; Endoplasmic reticulum; Oligosaccharyltransferase; Congenital disorders of glycosylation; DOLICHOL-LINKED OLIGOSACCHARIDE; HYDROXY AMINO-ACID; ASN-X-SER/THR; YEAST OLIGOSACCHARYLTRANSFERASE; SACCHAROMYCES-CEREVISIAE; CONGENITAL DISORDERS; ACCEPTOR SITES; RIBOPHORIN-I; OXIDOREDUCTASE ACTIVITY; QUALITY-CONTROL;

D O I：

10.1016/j.semcdb.2014.11.005

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

Asparagine linked glycosylation of proteins is an essential protein modification reaction in most eukaryotic organisms. N-linked oligosaccharides are important for protein folding and stability, biosynthetic quality control, intracellular traffic and the physiological function of many N-glycosylated proteins. In metazoan organisms, the oligosaccharyltransferase is composed of a catalytic subunit (STT3A or STT3B) and a set of accessory subunits. Duplication of the catalytic subunit gene allowed cells to evolve OST complexes that act sequentially to maximize the glycosylation efficiency of the large number of proteins that are glycosylated in metazoan organisms. We will summarize recent progress in understanding the mechanism of (a) cotranslational glycosylation by the translocation channel associated STT3A complex, (b) the role of the STT3B complex in mediating cotranslational or posttranslocational glycosylation of acceptor sites that have been skipped by the STT3A complex, and (c) the role of the oxidoreductase MagT1 in STT3B-dependent glycosylation of cysteine-proximal acceptor sites. (C) 2014 Elsevier Ltd. All rights reserved.

引用

页码：71 / 78

页数：8

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