Free and N-linked oligomannosides as markers of the quality control of newly synthesized glycoproteins

被引:18
作者
Cacan, R [1 ]
Verbert, A [1 ]
机构
[1] Univ Sci & Technol Lille, Chim Biol Lab, CNRS, UMR 111, F-59655 Villeneuve Dascq, France
关键词
N-glycosylation; endoplasmic reticulum; cytosol; oligomannoside trafficking; quality control; protein degradation;
D O I
10.1006/bbrc.1999.0549
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
It appears increasingly evident that the oligomannoside type N-glycans play important roles in the fate of newly synthesized glycoproteins in the rough endoplasmic reticulum. The variety of protein-bound oligomannoside isomers are involved in the quality control of glycoprotein, in their transport into the Golgis and probably as a degradation signal. A prerequisite of the degradation in the cytosol by the proteasome pathway is the release of the glycans as free oligomannosides. These oligomannosides are further processed in the cytosol into a peculiar isomer of Man(5)GlcNAc(1) which enters into the lysosome to be further degraded into monosaccharides. In this review, we will illustrate how the different species of N-linked and free oligomannosides either are involved or are markers of the quality control and fate of newly synthesized glycoproteins. (C) 1999 Academic Press.
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页码:1 / 5
页数:5
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