Regulation of N-Linked Core-Glycosylation

N-Linked glycosylation is one of the most common protein modifications and can have profound effects on protein expression and function. These effects often depend on the number and position of N-linked oligosaccharides added to a protein during core-glycosylation. While the sequon, Asn-X-Ser/Thr, s...

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Bibliographic Details
Published in:Trends in Glycoscience and Glycotechnology 1996/03/02, Vol.8(40), pp.115-130
Main Author: Shakin-Eshleman, Susan H.
Format: Article
Language:English
Subjects:
core-glycosylation
glycoprotein
N-linked glycosylation
protein signals
sequon
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Summary:N-Linked glycosylation is one of the most common protein modifications and can have profound effects on protein expression and function. These effects often depend on the number and position of N-linked oligosaccharides added to a protein during core-glycosylation. While the sequon, Asn-X-Ser/Thr, serves as a recognition signal for core-glycosylation, other protein signals must also control this process, since many Asn-X-Ser/Thr sequons are glycosylated inefficiently or are not glycosylated at all. A variety of experimental approaches have been used to define the signals which control core-glycosylation at specific Asn residues. These include comparisons of protein sequences near glycosylated and non-glycosylated sequons, use of sequon-containing peptides as oligosaccharide acceptors or inhibitors, and analysis of the glycosylation of sequons in recombinant proteins. Such studies reveal that a complex set of factors determines the efficiency of oligosaccharide addition at each Asn-X-Ser/Thr sequon. Amino acids near the Asn residue in a sequon can profoundly affect its oligosaccharide acceptor activity. A variety of other factors further modulate core-glycosylation efficiency by influencing the accessibility of sequons for glycosylation at a critical time during protein synthesis. Studies addressing these issues are reviewed.
ISSN:0915-7352
1883-2113
DOI:10.4052/tigg.8.115