Intracellular functions of N-linked glycans.

@article{Helenius2001IntracellularFO,
  title={Intracellular functions of N-linked glycans.},
  author={Ari Helenius and Markus Aebi},
  journal={Science},
  year={2001},
  volume={291 5512},
  pages={
          2364-9
        }
}
N-linked oligosaccharides arise when blocks of 14 sugars are added cotranslationally to newly synthesized polypeptides in the endoplasmic reticulum (ER). These glycans are then subjected to extensive modification as the glycoproteins mature and move through the ER via the Golgi complex to their final destinations inside and outside the cell. In the ER and in the early secretory pathway, where the repertoire of oligosaccharide structures is still rather small, the glycans play a pivotal role in… Expand
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References

SHOWING 1-10 OF 78 REFERENCES
Role of N-oligosaccharide endoplasmic reticulum processing reactions in glycoprotein folding and degradation.
TLDR
The interaction between CNX/CRT and a monoglucosylated glycan is one of the alternative mechanisms by which cells retain not yet properly folded glycoproteins in the ER and enhances folding efficiency by preventing protein aggregation and thus allowing intervention of classical chaperones and other folding-assisting proteins. Expand
The dolichol pathway of N-linked glycosylation.
TLDR
It is suggested that N-linked glycosylation in eukaryotes and in archaea share a common evolutionary origin and the function of the lipid carrier dolichol in oligosaccharide assembly is discussed. Expand
Carbohydrate moieties of glycoproteins. A re-evaluation of their function.
TLDR
It is proposed that the carbohydrate acts as a chemical ‘tag’ which, upon interaction with a specific intracellular membrane receptor, directs glycoproteins to specific cellular organelles following synthesis on the rough endoplasmic reticulum. Expand
Glycosidase inhibitors: inhibitors of N‐linked oligosaccharide processing
  • A. Elbein
  • Chemistry, Medicine
  • FASEB journal : official publication of the Federation of American Societies for Experimental Biology
  • 1991
TLDR
A number of alkaloid‐like compounds have been identified that are specific inhibitors of the glucosidases and mannosidases involved in glycoprotein processing, causing the formation of glycoproteins with glucose‐containing high mannose structures, or various high‐mannose or hybrid chains, depending on the site of inhibition. Expand
Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control.
TLDR
It is proposed that the ER contains a unique folding and quality control machinery in which calnexin acts as a chaperone that binds proteins with partially glucose-trimmed carbohydrate side chains, and glucosidases I and II serve as signal modifiers and UDP-glucose:glycoprotein glucosyltransferase, as a folding sensor. Expand
From peptidoglycan to glycoproteins: common features of lipid-linked oligosaccharide biosynthesis.
TLDR
The presence of dolichyl phosphate and a family of saturated isoprenoid lipids in Archaebacteria suggests a possible evolutionary link between the bacterial and eukaryotic systems. Expand
Lectins and traffic in the secretory pathway
TLDR
The mannose lectin ERGIC‐53 operates as a cargo receptor in transport of glycoproteins from ER to Golgi and the homologous lectin VIP36 may operate in quality control of glycosylation in the Golgi. Expand
Structure and biosynthesis of prokaryotic glycoproteins.
TLDR
The overall structure of the cell surface glycoprotein of halobacteria is thus reminiscent of animal proteoglycans and a functional role of the glycosaminoglycan chain in maintaining the rod shape of Halobacterium halob bacteria is discussed. Expand
Asparagine-linked Oligosaccharides Protect Lamp-1 and Lamp-2 from Intracellular Proteolysis*
TLDR
Endoglycosidase H treated cells provide direct evidence that Asn-linked oligosaccharides protect a subset of lysosomal membrane proteins from proteolytic digestion in intact cells. Expand
Protein glucosylation and its role in protein folding.
  • A. J. Parodi
  • Chemistry, Medicine
  • Annual review of biochemistry
  • 2000
TLDR
The lectin-monoglucosylated oligosaccharide interaction is one of the alternative ways by which cells retain improperly folded glycoproteins in the endoplasmic reticulum and increases folding efficiency, prevents premature glycoprotein oligomerization and degradation, and suppresses formation of non-native disulfide bonds. Expand
...
1
2
3
4
5
...