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Trends Biochem Sci. 2010 Feb;35(2):74-82. doi: 10.1016/j.tibs.2009.10.001. Epub 2009 Oct 21.

N-glycan structures: recognition and processing in the ER.

Author information

1
Institute of Microbiology, Department of Biology, Eidgenössische Technische Hochschule (ETH) Zürich, CH-8093 Zürich, Switzerland. markus.aebi@micro.biol.ethz.ch

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.

PMID:
19853458
DOI:
10.1016/j.tibs.2009.10.001
[Indexed for MEDLINE]

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