ArticleJournal of cell science2013
OST4 is a subunit of the mammalian oligosaccharyltransferase required for efficient N-glycosylation.
Article in Journal of cell science, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 35 citations in OpenAlex.
- Unraveling the Glycosylation Machinery ofInternational journal of molecular sciences · 2026Article
- Taxonomic context and genomic architecture jointly shape expression divergence across animals.Evolution; international journal of organic evolution · 2026Article
- Genome-Wide Identification of Genomic Regions Associated with Body Weight and Morphometric Traits in Awassi Sheep.Animals : an open access journal from MDPI · 2026Article
- Combining multi-omics analysis methods to identify biomarkers for mitophagy involved in immune checkpoint inhibitors-related myocarditis.Frontiers in immunology · 2026Article
- Taxonomic context and genomic architecture jointly shape expression divergence across animals.bioRxiv : the preprint server for biology · 2025Article
- Functional modules predict cancer-relevant genetic interactions in mammalian cells.bioRxiv : the preprint server for biology · 2025Article
- An integrative multitiered computational analysis for better understanding the structure and function of 85 miniproteins.NAR genomics and bioinformatics · 2025Article
- The oligosaccharyltransferase complex is an essential component of multiple myeloma plasma cells.Molecular therapy. Oncology · 2025Article
- Review and metabolomic profiling of unsolved case reveals newly reported autosomal dominant congenital disorder of glycosylation, type Iw formerly thought to only be an autosomal recessive condition.Molecular genetics and metabolism reports · 2024Article
- Detecting early-warning biomarkers associated with heart-exosome genetic-signature for acute myocardial infarction: A source-tracking study of exosome.Journal of cellular and molecular medicine · 2024Article
- Identification and validation of extracellular vesicle reference genes for the normalization of RT-qPCR data.Journal of extracellular vesicles · 2024Article
- Transcriptional profiling of human cartilage endplate cells identifies novel genes and cell clusters underlying degenerated and non-degenerated phenotypes.Arthritis research & therapy · 2024Article
- Squalene through Its Post-Squalene Metabolites Is a Modulator of Hepatic Transcriptome in Rabbits.International journal of molecular sciences · 2022Article
- Identification of methylation signatures associated with CAR T cell in B-cell acute lymphoblastic leukemia and non-hodgkin's lymphoma.Frontiers in oncology · 2022Article
- Review
- Posttranslational insertion of small membrane proteins by the bacterial signal recognition particle.PLoS biology · 2020Article
- Oligosaccharyltransferase: A Gatekeeper of Health and Tumor Progression.International journal of molecular sciences · 2019Review
- iTRAQ-Based Comparative Proteomic Analysis Provides Insights into Molecular Mechanisms of Salt Tolerance in Sugar Beet (International journal of molecular sciences · 2018Article
- In silico analyses of protein glycosylating genes in the helminth Fasciola hepatica (liver fluke) predict protein-linked glycan simplicity and reveal temporally-dynamic expression profiles.Scientific reports · 2018Article
- Selenoprotein T is a novel OST subunit that regulates UPR signaling and hormone secretion.EMBO reports · 2017Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The eukaryotic oligosaccharyltransferase (OST) is a membrane-embedded protein complex that catalyses the N-glycosylation of nascent polypeptides in the lumen of the endoplasmic reticulum (ER), a highly conserved biosynthetic process that enriches protein structure and function. All OSTs contain a homologue of the catalytic STT3 subunit, although in many cases this is assembled with several additional components that influence function. In S. cerevisiae, one such component is Ost4p, an extremely small membrane protein that appears to stabilise interactions between subunits of assembled OST complexes. OST4 has been identified as a putative human homologue, but to date neither its relationship to the OST complex, nor its role in protein N-glycosylation, have been directly addressed. Here, we establish that OST4 is assembled into native OST complexes containing either the catalytic STT3A or STT3B isoforms. Co-immunoprecipitation studies suggest that OST4 associates with both STT3 isoforms and with ribophorin I, an accessory subunit of mammalian OSTs. These presumptive interactions are perturbed by a single amino acid change in the transmembrane region of OST4. Using siRNA knockdowns and native gel analysis, we show that OST4 plays an important role in maintaining the stability of native OST complexes. Hence, upon OST4 depletion well-defined OST complexes are partially destabilised and a novel ribophorin I-containing subcomplex can be detected. Strikingly, cells depleted of either OST4 or STT3A show a remarkably similar defect in the N-glycosylation of endogenous prosaposin. We conclude that OST4 most likely promotes co-translational N-glycosylation by stabilising STT3A-containing OST isoforms.
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