ArticleMolecular & cellular proteomics : MCP2014
Oligosaccharyltransferase subunits bind polypeptide substrate to locally enhance N-glycosylation.
Article in Molecular & cellular proteomics : MCP, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 12 citations in OpenAlex.
- An Update on XMEN Disease.Journal of clinical immunology · 2020Review
- Defective glycosylation and multisystem abnormalities characterize the primary immunodeficiency XMEN disease.The Journal of clinical investigation · 2020Article
- Quantitative Profiling of N-linked Glycosylation Machinery in YeastMolecular & cellular proteomics : MCP · 2018Article
- Diminished Ost3-dependent N-glycosylation of the BiP nucleotide exchange factor Sil1 is an adaptive response to reductive ER stress.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Cellular Consequences of Diminished Protein O-Mannosyltransferase Activity in Baker's Yeast.International journal of molecular sciences · 2017Article
- Plant protein glycosylation.Glycobiology · 2016Review
- SWATH-MS Glycoproteomics Reveals Consequences of Defects in the Glycosylation Machinery.Molecular & cellular proteomics : MCP · 2016Article
- N-glycoprotein macroheterogeneity: biological implications and proteomic characterization.Glycoconjugate journal · 2016Review
- Substrate specificities and reaction kinetics of the yeast oligosaccharyltransferase isoforms.The Journal of biological chemistryArticle
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Oligosaccharyltransferase is a multiprotein complex that catalyzes asparagine-linked glycosylation of diverse proteins. Using yeast genetics and glycoproteomics, we found that transient interactions between nascent polypeptide and Ost3p/Ost6p, homologous subunits of oligosaccharyltransferase, were able to modulate glycosylation efficiency in a site-specific manner in vivo. These interactions were driven by hydrophobic and electrostatic complementarity between amino acids in the peptide-binding groove of Ost3p/Ost6p and the sequestered stretch of substrate polypeptide. Based on this dependence, we used in vivo scanning mutagenesis and in vitro biochemistry to map the precise interactions that affect site-specific glycosylation efficiency. We conclude that transient binding of substrate polypeptide by Ost3p/Ost6p increases glycosylation efficiency at asparagines proximal and C-terminal to sequestered sequences. We detail a novel mode of interaction between translocating nascent polypeptide and oligosaccharyltransferase in which binding to Ost3p/Ost6p segregates a short flexible loop of glycosylation-competent polypeptide substrate that is delivered to the oligosaccharyltransferase active site for efficient modification.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.