ArticleThe Journal of biological chemistry2013
Eukaryotic oligosaccharyltransferase generates free oligosaccharides during N-glycosylation.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- Cytosolic Peptide: N-Glycanase (NGLY1)-from Basic Biology to Genetic Disorder, NGLY1 Deficiency.Advances in experimental medicine and biology · 2026Review
- Free oligosaccharides in serum.BBA advances · 2025Article
- Organellar homeostasis and innate immune sensing.Nature reviews. Immunology · 2022Review
- The structure of an archaeal oligosaccharyltransferase provides insight into the strict exclusion of proline from the N-glycosylation sequon.Communications biology · 2021Article
- Uncoupling the hydrolysis of lipid-linked oligosaccharide from the oligosaccharyl transfer reaction by point mutations in yeast oligosaccharyltransferase.The Journal of biological chemistry · 2020Article
- Cryo-EM structure of fission yeast tetrameric α-mannosidase Ams1.FEBS open bio · 2020Article
- Toolbox Accelerating Glycomics (TAG): Glycan Annotation from MALDI-TOF MS Spectra and Mapping Expression Variation to Biosynthetic Pathways.Biomolecules · 2020Article
- Free glycans derived fromThe Journal of biological chemistry · 2019Article
- A bioactive mammalian disaccharide associated with autoimmunity activates STING-TBK1-dependent immune response.Nature communications · 2019Article
- A Radioisotope-free Oligosaccharyltransferase Assay Method.Bio-protocol · 2019Article
- Structure of bacterial oligosaccharyltransferase PglB bound to a reactive LLO and an inhibitory peptide.Scientific reports · 2018Article
- Mammalian STT3A/B oligosaccharyltransferases segregate N-glycosylation at the translocon from lipid-linked oligosaccharide hydrolysis.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Occurrence of complex type free N-glycans with a single GlcNAc residue at the reducing termini in the fresh-water plant, Egeria densa.Glycoconjugate journal · 2017Article
- Brefeldin A promotes the appearance of oligosaccharyl phosphates derived from Glc3Man9GlcNAc2-PP-dolichol within the endomembrane system of HepG2 cells.Journal of lipid research · 2016Article
- Demonstration of an oligosaccharide-diphosphodolichol diphosphatase activity whose subcellular localization is different than those of dolichyl-phosphate-dependent enzymes of the dolichol cycle.Journal of lipid research · 2016Article
- Non-lysosomal Degradation of Singly Phosphorylated Oligosaccharides Initiated by the Action of a Cytosolic Endo-β-N-acetylglucosaminidase.The Journal of biological chemistry · 2016Article
- The cytoplasmic peptide:N-glycanase (NGLY1) - Structure, expression and cellular functions.Gene · 2016Review
- Article
- Generation and degradation of free asparagine-linked glycans.Cellular and molecular life sciences : CMLS · 2015Review
- Substrate specificities and reaction kinetics of the yeast oligosaccharyltransferase isoforms.The Journal of biological chemistryArticle
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6 authors.
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Abstract
Asparagine (N)-linked glycosylation regulates numerous cellular activities, such as glycoprotein quality control, intracellular trafficking, and cell-cell communications. In eukaryotes, the glycosylation reaction is catalyzed by oligosaccharyltransferase (OST), a multimembrane protein complex that is localized in the endoplasmic reticulum (ER). During N-glycosylation in the ER, the protein-unbound form of oligosaccharides (free oligosaccharides; fOSs), which is structurally related to N-glycan, is released into the ER lumen. However, the enzyme responsible for this process remains unidentified. Here, we demonstrate that eukaryotic OST generates fOSs. Biochemical and genetic analyses using mutant strains of Saccharomyces cerevisiae revealed that the generation of fOSs is tightly correlated with the N-glycosylation activity of OST. Furthermore, we present evidence that the purified OST complex can generate fOSs by hydrolyzing dolichol-linked oligosaccharide, the glycan donor substrate for N-glycosylation. The heterologous expression of a single subunit of OST from the protozoan Leishmania major in S. cerevisiae demonstrated that this enzyme functions both in N-glycosylation and generation of fOSs. This study provides insight into the mechanism of PNGase-independent formation of fOSs.
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