ArticleNature chemical biology2015
O-GlcNAc occurs cotranslationally to stabilize nascent polypeptide chains.
Article in Nature chemical biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.
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Who cites it
69 citing papers in PubMed.
- Cross-talk between glycosylation pathways: Mechanistic insights and implications for human diseases.Molecular metabolism · 2026Review
- Dissecting the Mechanisms Underlying Substrate Recognition and Functional Regulation of O-GlcNAc Cycling Enzymes.ACS chemical biology · 2025Review
- O-GlcNAc modulation of nuclear pore complexes orchestrates mRNA export efficiency.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- O-GlcNAcylation of the intellectual disability protein DDX3X exerts proteostatic cell cycle control.Open biology · 2025Article
- O-GlcNAc modification of HSP27 alters its protein interactions and promotes refolding of proteins through the BAG3/HSP70 co-chaperone.Protein science : a publication of the Protein Society · 2024Article
- Review
- Dissecting OGT's TPR domain to identify determinants of cellular function.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- O-GlcNAc Modification Alters the Chaperone Activity of HSP27 Charcot-Marie-Tooth Type 2 (CMT2) Variants in a Mutation-Selective Fashion.ACS chemical biology · 2023Article
- Deciphering the Properties and Functions of Glycoproteins Using Quantitative Proteomics.Journal of proteome research · 2023Review
- Transient receptor potential canonical type 6 (TRPC6) O-GlcNAcylation at Threonine-221 plays potent role in channel regulation.iScience · 2023Article
- Combining Selective Enrichment and a Boosting Approach to Globally and Site-Specifically Characterize Protein Co-translationalAnalytical chemistry · 2023Article
- Protein-Peptide Turnover Profiling reveals the order of PTM addition and removal during protein maturation.Nature communications · 2022Article
- Review
- Spatial and temporal proteomics reveals the distinct distributions and dynamics of O-GlcNAcylated proteins.Cell reports · 2022Article
- Discovery of a New Drug-like Series of OGT Inhibitors by Virtual Screening.Molecules (Basel, Switzerland) · 2022Article
- Contribution of the STAT Family of Transcription Factors to the Expression of the Serotonin 2B (HTR2B) Receptor in Human Uveal Melanoma.International journal of molecular sciences · 2022Article
- Writing and erasing O-GlcNAc from target proteins in cells.Biochemical Society transactions · 2021Article
- Discovery proteomics defines androgen-regulated glycoprotein networks in prostate cancer cells, as well as putative biomarkers of prostatic diseases.Scientific reports · 2021Article
- Role and Function of O-GlcNAcylation in Cancer.Cancers · 2021Review
- Advances in chemical probing of proteinChemical Society reviews · 2021Review
9 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors.
Funding
Abstract
Nucleocytoplasmic glycosylation of proteins with O-linked N-acetylglucosamine residues (O-GlcNAc) is recognized as a conserved post-translational modification found in all metazoans. O-GlcNAc has been proposed to regulate diverse cellular processes. Impaired cellular O-GlcNAcylation has been found to lead to decreases in the levels of various proteins, which is one mechanism by which O-GlcNAc seems to exert its varied physiological effects. Here we show that O-GlcNAcylation also occurs cotranslationally. This process protects nascent polypeptide chains from premature degradation by decreasing cotranslational ubiquitylation. Given that hundreds of proteins are O-GlcNAcylated within cells, our findings suggest that cotranslational O-GlcNAcylation may be a phenomenon regulating proteostasis of an array of nucleocytoplasmic proteins. These findings set the stage to assess whether O-GlcNAcylation has a role in protein quality control in a manner that bears similarity with the role played by N-glycosylation within the secretory pathway.
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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.