| Literature DB >> 19853458 |
Markus Aebi1, Riccardo Bernasconi, Simone Clerc, Maurizio Molinari.
Abstract
The processing of N-linked 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 N-linked 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. (c) 2009 Elsevier Ltd. All rights reserved.Entities:
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Year: 2009 PMID: 19853458 DOI: 10.1016/j.tibs.2009.10.001
Source DB: PubMed Journal: Trends Biochem Sci ISSN: 0968-0004 Impact factor: 13.807