N-linked carbohydrates act as lumenal maturation and quality control protein tags

被引：8

作者：

Daniels, R ^{[1
]}

Svedine, S ^{[1
]}

Hebert, DN ^{[1
]}

机构：

[1] Univ Massachusetts, Dept Biochem & Mol Biol, Program Mol & Cellular Biol, Amherst, MA 01003 USA

来源：

CELL BIOCHEMISTRY AND BIOPHYSICS | 2004年 / 41卷 / 01期

关键词：

secretory pathway; calnexin; calreticulin; glycosylation; ERAD; endoplasmic reticulum;

D O I：

10.1385/CBB:41:1:113

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：

Protein modifications such as ubiquitination and phosphorylation commonly serve as sorting tags that control the trafficking and stability of a protein within the cytosol. In recent years, N-linked glycans have emerged as key protein modifications for eukaryotic secretory proteins. These modifications support the recruitment of molecular chaperones and sorting receptors, which recognize specific glycoforms. Therefore, glycanases and carbohydrate transferases work in concert with lectin chaperones and receptors to aid in the maturation and quality control of glycoproteins.

引用

页码：113 / 137

页数：25

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