N-glycan structures: recognition and processing in the ER
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.
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Keywords: 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
Record created on 2011-12-16, modified on 2016-08-09