2001/03/23 by Ari Helenius, and Markus Aebi · 3 citations
Biochemistry, Genetics and Molecular Biology · Chemistry · #Glycosylation and Glycoproteins Research #Carbohydrate Chemistry and Synthesis #Cellular transport and secretion
paper · doi:10.1126/science.291.5512.2364
openalex publication_date 2001/03/23 · openalex created_date 2025/10/10 · openalex updated_date 2026/07/28
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.