N-glycan structure dictates extension of protein folding or onset of disposal

被引:230
作者
Molinari, Maurizio [1 ]
机构
[1] Inst Res Biomed, CH-6500 Bellinzona, Switzerland
关键词
D O I
10.1038/nchembio880
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 the site of folding for proteins that are resident in the ER or that are destined for the Golgi, endosomes, lysosomes, the plasma membrane, or secretion. Cotranslational addition of preassembled glucose(3)-mannose(9)-N-acetylglucosamine(2) core oligosaccharides (N-glycosylation) is a common event for polypeptides synthesized in this compartment. Protein-bound oligosaccharides are exposed to several ER glycanases that sequentially remove terminal glucose or mannose residues. Their activity must be tightly regulated because the N-glycan composition determines whether the associated protein is subjected to folding attempts in the ER lumen or whether it is retrotranslocated into the cytosol and degraded.
引用
收藏
页码:313 / 320
页数:8
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