N-glycan structures: recognition and processing in the ER

被引:344
作者
Aebi, Markus [1 ]
Bernasconi, Riccardo [2 ]
Clerc, Simone [1 ]
Molinari, Maurizio [2 ,3 ]
机构
[1] ETH, Dept Biol, Inst Microbiol, CH-8093 Zurich, Switzerland
[2] Inst Biomed Res, CH-6500 Bellinzona, Switzerland
[3] Ecole Polytech Fed Lausanne, Sch Life Sci, CH-1015 Lausanne, Switzerland
基金
瑞士国家科学基金会;
关键词
RETICULUM-ASSOCIATED DEGRADATION; GLUCOSE-GLYCOPROTEIN-GLUCOSYLTRANSFERASE; UNFOLDED PROTEIN RESPONSE; UBIQUITIN LIGASE COMPLEX; MANNOSIDASE-LIKE PROTEIN; SHORT-LIVED VARIANT; ENDOPLASMIC-RETICULUM; QUALITY-CONTROL; MISFOLDED GLYCOPROTEINS; SACCHAROMYCES-CEREVISIAE;
D O I
10.1016/j.tibs.2009.10.001
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 processing of Winked glycans determines secretory protein homeostasis in the eukaryotic cell. Folding and degradation of glycoproteins in the endoplasmic reticulum (ER) are regulated by molecular chaperones and enzymes recruited by specific oligosaccharide structures. Recent findings have identified several components of this protein quality control system that specifically modify Winked glycans, thereby generating oligosaccharide structures recognized by carbohydrate-binding proteins, lectins. In turn, lectins direct newly synthesized polypeptides to the folding, secretion or degradation pathways. The "glyco-code of the ER" displays the folding status of a multitude of cargo proteins. Deciphering this code will be instrumental in understanding protein homeostasis regulation in eukaryotic cells and for intervention because such processes can have crucial importance for clinical and industrial applications.
引用
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页码:74 / 82
页数:9
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