ArticleThe Journal of biological chemistry2008
Regulation of the O-linked beta-N-acetylglucosamine transferase by insulin signaling.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 116 papers, 1 of them a synthesis that pooled it.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
116 citing papers in PubMed, 1 synthesis or guideline pooled it, 173 citations in OpenAlex.
- Tools for investigating O-GlcNAc in signaling and other fundamental biological pathways.The Journal of biological chemistry · 2024Pooled it
- Deciphering O‑GlcNAc-Dependent Signaling Via Integrated Proteomics and Phosphoproteomics.ACS omega · 2026Article
- Notch1 O-GlcNAcylation drives tumor stemness and mechanoadaptation to a stiff microenvironment and promotes chordoma recurrence.The Journal of clinical investigation · 2026Article
- Advances and challenges in the mechanistic understanding of beta-cell dysfunction in gestational diabetes mellitus.Journal of animal science · 2026Review
- ACE-mediated Glycosylation Stabilizes PSAP To Promote GPR37-dependent Macrophage-Nucleus Pulposus Cells Crosstalk and TGFβ Signaling in Alleviating Intervertebral Disc Degeneration.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Protein O-GlcNAcylation in reproductive biology and the impact of metabolic disease.Human reproduction update · 2025Review
- O-GlcNAc transferase plays dual antiviral roles by integrating innate immunity and lipid metabolism.Nature communications · 2025Article
- O-GlcNAcylation: Sagacious Orchestrator of Bone-, Joint-, and Spine-Related Diseases.Journal of proteome research · 2025Review
- The role of protein O-GlcNAcylation in diabetic cardiomyopathy.Biochemical Society transactions · 2024Review
- Posttranslational Modifications ofPharmacological reviews · 2024Review
- Article
- The post-translational modification O-GlcNAc is a sensor and regulator of metabolism.Open biology · 2024Review
- Organization of a functional glycolytic metabolon on mitochondria for metabolic efficiency.Nature metabolism · 2024Article
- Neurodevelopmental defects in a mouse model of O-GlcNAc transferase intellectual disability.Disease models & mechanisms · 2024Article
- vNARs as Neutralizing Intracellular Therapeutic Agents: Glioblastoma as a Target.Antibodies (Basel, Switzerland) · 2024Review
- Regulation of protein O-GlcNAcylation by circadian, metabolic, and cellular signals.The Journal of biological chemistry · 2024Review
- Review
- The O-GlcNAc dichotomy: when does adaptation become pathological?Clinical science (London, England : 1979) · 2023Review
- Phosphoinositides and intracellular calcium signaling: novel insights into phosphoinositides and calcium coupling as negative regulators of cellular signaling.Experimental & molecular medicine · 2023Review
- Article
56 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
O-Linked beta-N-acetylglucosamine (O-GlcNAc) transferase (OGT) catalyzes the addition of O-linked beta-N-acetylglucosamine (O-GlcNAc) onto serine and threonine residues in response to stimuli or stress analogous to phosphorylation by Ser/Thr-kinases. Like protein phosphatases, OGT appears to be targeted to myriad specific substrates by transiently interacting with specific targeting subunits. Here, we show that OGT is activated by insulin signaling. Insulin treatment of 3T3-L1 adipocytes stimulates both tyrosine phosphorylation and catalytic activity of OGT. A subset of OGT co-immunoprecipitates with the insulin receptor. Insulin stimulates purified insulin receptor to phosphorylate OGT in vitro. OGT is a competitive substrate with reduced and carboxyamidomethylated lysozyme (RCAM-lysozyme), a well characterized insulin receptor substrate. Insulin stimulation of 3T3-L1 adipocytes results in a partial translocation of OGT from the nucleus to the cytoplasm. The insulin activation of OGT results in increased O-GlcNAc modification of OGT and other proteins including, signal transducer and activator of transcription 3 (STAT3). We conclude that insulin stimulates the tyrosine phosphorylation and activity of OGT.
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What OpenQuestion holds
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.