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Semin Cell Dev Biol. 2015 May;41:71-8. doi: 10.1016/j.semcdb.2014.11.005. Epub 2014 Nov 24.

Cotranslational and posttranslocational N-glycosylation of proteins in the endoplasmic reticulum.

Author information

1
Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, MA, 01605, United States.
2
Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, MA, 01605, United States. Electronic address: reid.gilmore@umassmed.edu.

Abstract

Asparagine linked glycosylation of proteins is an essential protein modification reaction in most eukaryotic organisms. N-linked oligosaccharides are important for protein folding and stability, biosynthetic quality control, intracellular traffic and the physiological function of many N-glycosylated proteins. In metazoan organisms, the oligosaccharyltransferase is composed of a catalytic subunit (STT3A or STT3B) and a set of accessory subunits. Duplication of the catalytic subunit gene allowed cells to evolve OST complexes that act sequentially to maximize the glycosylation efficiency of the large number of proteins that are glycosylated in metazoan organisms. We will summarize recent progress in understanding the mechanism of (a) cotranslational glycosylation by the translocation channel associated STT3A complex, (b) the role of the STT3B complex in mediating cotranslational or posttranslocational glycosylation of acceptor sites that have been skipped by the STT3A complex, and (c) the role of the oxidoreductase MagT1 in STT3B-dependent glycosylation of cysteine-proximal acceptor sites.

KEYWORDS:

Asparagine linked glycosylation; Congenital disorders of glycosylation; Endoplasmic reticulum; Oligosaccharyltransferase

PMID:
25460543
PMCID:
PMC4442082
DOI:
10.1016/j.semcdb.2014.11.005
[Indexed for MEDLINE]
Free PMC Article

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