ArticleProceedings of the National Academy of Sciences of the United States of America2009
Oligosaccharyltransferase directly binds to ribosome at a location near the translocon-binding site.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed.
- An Intrabody against B-Cell Receptor-Associated Protein 31 (BAP31) Suppresses the Glycosylation of the Epithelial Cell-Adhesion Molecule (EpCAM) via Affecting the Formation of the Sec61-Translocon-Associated Protein (TRAP) Complex.International journal of molecular sciences · 2023Article
- Sweet Modifications Modulate Plant Development.Biomolecules · 2021Review
- Distinct roles and actions of protein disulfide isomerase family enzymes in catalysis of nascent-chain disulfide bond formation.iScience · 2021Article
- mRNA Targeting, Transport and Local Translation in Eukaryotic Cells: From the Classical View to a Diversity of New Concepts.Molecular biology · 2021Article
- Quantitative Proteomics Links the LRRC59 Interactome to mRNA Translation on the ER Membrane.Molecular & cellular proteomics : MCP · 2020Article
- The SH3 domain in the fucosyltransferase FUT8 controls FUT8 activity and localization and is essential for core fucosylation.The Journal of biological chemistry · 2020Article
- Structural Insight into the Mechanism ofBiomolecules · 2020Review
- Oligosaccharyltransferase: A Gatekeeper of Health and Tumor Progression.International journal of molecular sciences · 2019Review
- Asparagine-linked glycosylation is not directly coupled to protein translocation across the endoplasmic reticulum inMolecular biology of the cell · 2019Article
- Heterogeneous translational landscape of the endoplasmic reticulum revealed by ribosome proximity labeling and transcriptome analysis.The Journal of biological chemistry · 2019Article
- Folding and Misfolding of Human Membrane Proteins in Health and Disease: From Single Molecules to Cellular Proteostasis.Chemical reviews · 2019Article
- Oligosaccharyltransferase structures provide novel insight into the mechanism of asparagine-linked glycosylation in prokaryotic and eukaryotic cells.Glycobiology · 2019Review
- TPR-containing proteins control protein organization and homeostasis for the endoplasmic reticulum.Critical reviews in biochemistry and molecular biology · 2019Review
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- A Comprehensive Analysis of Replicative Lifespan in 4,698 Single-Gene Deletion Strains Uncovers Conserved Mechanisms of Aging.Cell metabolism · 2015Article
- Generation and degradation of free asparagine-linked glycans.Cellular and molecular life sciences : CMLS · 2015Review
- Diversity and selectivity in mRNA translation on the endoplasmic reticulum.Nature reviews. Molecular cell biology · 2015Review
- Oligosaccharyltransferase subunits bind polypeptide substrate to locally enhance N-glycosylation.Molecular & cellular proteomics : MCP · 2014Article
- Eukaryotic oligosaccharyltransferase generates free oligosaccharides during N-glycosylation.The Journal of biological chemistry · 2013Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Oligosaccharyltransferase (OT) transfers high mannose-type glycans to the nascent polypeptides that are translated by the membrane-bound ribosome and translocated into the lumen of the endoplasmic reticulum through the Sec61 translocon complex. In this article, we show that purified ribosomes and OT can form a binary complex with a stoichiometry of approximately 1 to 1 in the presence of detergent. We present evidence that OT may bind to the large ribosomal subunit near the site where nascent polypeptides exit. We further show that OT and the Sec61 complex can simultaneously bind to ribosomes in vitro. Based on existing data and our findings, we propose that cotranslational translocation and N-glycosylation of nascent polypeptides are mediated by a ternary supramolecular complex consisting of OT, the Sec61 complex, and ribosomes.
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Registered trials
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