Non-lysosomal degradation pathway for N-linked glycans and dolichol-linked oligosaccharides

被引:30
|
作者
Suzuki, Tadashi [1 ]
Harada, Yoichiro [1 ]
机构
[1] RIKEN, Global Res Cluster, RIKEN Max Planck Joint Res Ctr Syst Chem Biol, Glycometabolome Team,Syst Glycobiol Res Grp, Wako, Saitama 3510198, Japan
关键词
Free oligosaccharides; Phosphorylated oligosaccharides; Non-lysosomal degradation; Peptide:N-glycanase; Oligosaccharyltransferase; Pyrophosphatase; RETICULUM-ASSOCIATED DEGRADATION; POLYMANNOSE-TYPE OLIGOSACCHARIDES; PROTEIN-PROTEIN INTERACTION; ENDOPLASMIC-RETICULUM; ALPHA-MANNOSIDASE; SACCHAROMYCES-CEREVISIAE; GLYCOPROTEIN-BIOSYNTHESIS; CYTOPLASMIC PEPTIDE; QUALITY-CONTROL; EUKARYOTIC OLIGOSACCHARYLTRANSFERASE;
D O I
10.1016/j.bbrc.2014.05.075
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
There is growing evidence that asparagine (N)-linked glycans play pivotal roles in protein folding and intra- or intercellular trafficking of N-glycosylated proteins. During the N-glycosylation of proteins, significant amounts of free oligosaccharides (fOSs) and phosphorylated oligosaccharides (POSs) are generated at the endoplasmic reticulum (ER) membrane by unclarified mechanisms. fOSs are also formed in the cytosol by the enzymatic deglycosylation of misfolded glycoproteins destined for proteasomal degradation. This article summarizes the current knowledge of the molecular and regulatory mechanisms underlying the formation of fOSs and POSs in mammalian cells and Saccharomyces cerevisiae. (C) 2014 Elsevier Inc. All rights reserved.
引用
收藏
页码:213 / 219
页数:7
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