Intracellular Functions of N-Linked Glycans
- 23 March 2001
- journal article
- review article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 291 (5512), 2364-2369
- https://doi.org/10.1126/science.291.5512.2364
Abstract
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 protein folding, oligomerization, quality control, sorting, and transport. They are used as universal “tags” that allow specific lectins and modifying enzymes to establish order among the diversity of maturing glycoproteins. In the Golgi complex, the glycans acquire more complex structures and a new set of functions. The division of synthesis and processing between the ER and the Golgi complex represents an evolutionary adaptation that allows efficient exploitation of the potential of oligosaccharides.Keywords
This publication has 74 references indexed in Scilit:
- Endoplasmic Reticulum (ER)-associated Degradation of Misfolded N-Linked Glycoproteins Is Suppressed upon Inhibition of ER Mannosidase IPublished by Elsevier BV ,2000
- Probing the Three-Dimensional Structure of Human CalreticulinBiochemistry, 2000
- The Debate about Transport in the Golgi—Two Sides of the Same Coin?Cell, 2000
- Lectins and traffic in the secretory pathwayFEBS Letters, 2000
- III. Biochemistry of S-layersFEMS Microbiology Reviews, 1997
- ERGIC-53, a Membrane Protein of the Endoplasmic Reticulum-Golgi Intermediate Compartment, Is Identical to MR60, an Intracellular Mannose-specific Lectin of Myelomonocytic CellsPublished by Elsevier BV ,1995
- Vesicular stomatitis virus glycoprotein is sorted and concentrated during export from the endoplasmic reticulumCell, 1994
- Protein degradation in the endoplasmic reticulumCell, 1990
- Carbohydrate moieties of glycoproteins a re-evaluation of their functionBiochimica et Biophysica Acta (BBA) - Reviews on Biomembranes, 1982
- Intracellular Aspects of the Process of Protein SynthesisScience, 1975