Roles of N-Linked Glycans in the Endoplasmic Reticulum
École Polytechnique Fédérale de Lausanne
Abstract
From a process involved in cell wall synthesis in archaea and some bacteria, N-linked glycosylation has evolved into the most common covalent protein modification in eukaryotic cells. The sugars are added to nascent proteins as a core oligosaccharide unit, which is then extensively modified by removal and addition of sugar residues in the endoplasmic reticulum (ER) and the Golgi complex. It has become evident that the modifications that take place in the ER reflect a spectrum of functions related to glycoprotein folding, quality control, sorting, degradation, and secretion. The glycans not only promote folding directly by stabilizing polypeptide structures but also indirectly by serving as recognition "tags"…
Citation impact
- FWCI
- 43.03
- Percentile
- 100%
- References
- 182
Authors
2Topics & keywords
- Calnexin
- Endoplasmic reticulum
- Golgi apparatus
- Glycoprotein
- Glycosylation
- Calreticulin
- Glycan
- Endoplasmic-reticulum-associated protein degradation