ArticleProceedings of the National Academy of Sciences of the United States of America2021
Mammalian cell proliferation requires noncatalytic functions of O-GlcNAc transferase.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers, 1 of them a synthesis that pooled it.
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Who cites it
48 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Tools for investigating O-GlcNAc in signaling and other fundamental biological pathways.The Journal of biological chemistry · 2024Pooled it
- Chemical biology tools for the O-GlcNAc modification: Determining systems-level functions and druggability.Current opinion in chemical biology · 2026Review
- Systematic mapping of O-GlcNAc transferase and O-GlcNAcase defines disease-associated variants.The Journal of biological chemistry · 2026Article
- FoTO1 orchestrates Taxol biosynthesis through catalytic and non-catalytic mechanisms.bioRxiv : the preprint server for biology · 2026Article
- Targeted stress granule regulation by engineering a non-catalytic O-GlcNAc transferase.Nature communications · 2026Article
- OGT-Mediated O-GlcNAcylation Stabilizes c-Myc Activity and Promotes Chemoresistance in Triple-Negative Breast Cancer.The breast journal · 2026Article
- Dissecting the Mechanisms Underlying Substrate Recognition and Functional Regulation of O-GlcNAc Cycling Enzymes.ACS chemical biology · 2025Review
- The Glyco-Switch of life: O-GlcNAcylation in cell fate decision.Glycobiology · 2025Review
- O‑GlcNAcylation as an emerging molecular target for cholangiocarcinoma therapy (Review).Oncology reports · 2025Review
- Identification and characterization of O-GlcNAc modifications of a conserved orthopoxvirus core protein.Journal of virology · 2025Article
- Perturbing nuclear glycosylation in the mouse preimplantation embryo slows down embryonic development.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Photoactivatable O-GlcNAc Transferase Library Enables Covalent Chemical Capture of Solvent-Exposed TPR Domain Interactions.Chembiochem : a European journal of chemical biology · 2025Article
- Genetic gradual reduction of OGT activity unveils the essential role of O-GlcNAc in the mouse embryo.PLoS genetics · 2025Article
- Article
- Identification of a Polypeptide Inhibitor ofJournal of the American Chemical Society · 2024Article
- The roles of OGT and its mechanisms in cancer.Cell & bioscience · 2024Review
- O-GlcNAc transferase congenital disorder of glycosylation (OGT-CDG): Potential mechanistic targets revealed by evaluating the OGT interactome.The Journal of biological chemistry · 2024Review
- Neuronal activity-driven O-GlcNAcylation promotes mitochondrial plasticity.Developmental cell · 2024Article
- The non-catalytic domains of O-GlcNAc cycling enzymes present new opportunities for function-specific control.Current opinion in chemical biology · 2024Review
- 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
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Authors and funding
10 authors.
Funding
Abstract
O-GlcNAc transferase (OGT), found in the nucleus and cytoplasm of all mammalian cell types, is essential for cell proliferation. Why OGT is required for cell growth is not known. OGT performs two enzymatic reactions in the same active site. In one, it glycosylates thousands of different proteins, and in the other, it proteolytically cleaves another essential protein involved in gene expression. Deconvoluting OGT's myriad cellular roles has been challenging because genetic deletion is lethal; complementation methods have not been established. Here, we developed approaches to replace endogenous OGT with separation-of-function variants to investigate the importance of OGT's enzymatic activities for cell viability. Using genetic complementation, we found that OGT's glycosyltransferase function is required for cell growth but its protease function is dispensable. We next used complementation to construct a cell line with degron-tagged wild-type OGT. When OGT was degraded to very low levels, cells stopped proliferating but remained viable. Adding back catalytically inactive OGT rescued growth. Therefore, OGT has an essential noncatalytic role that is necessary for cell proliferation. By developing a method to quantify how OGT's catalytic and noncatalytic activities affect protein abundance, we found that OGT's noncatalytic functions often affect different proteins from its catalytic functions. Proteins involved in oxidative phosphorylation and the actin cytoskeleton were especially impacted by the noncatalytic functions. We conclude that OGT integrates both catalytic and noncatalytic functions to control cell physiology.
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