ArticleThe Journal of biological chemistry2011
Hyperglycemia-induced O-GlcNAcylation and truncation of 4E-BP1 protein in liver of a mouse model of type 1 diabetes.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 29 citations in OpenAlex.
- Cell cycle regulation in cancer cells by O-GlcNAcylation.Glycoconjugate journal · 2025Review
- Retinal Protein O-GlcNAcylation and the Ocular Renin-angiotensin System: Signaling Cross-roads in Diabetic Retinopathy.Current diabetes reviews · 2022Article
- Feedback Regulation ofInternational journal of molecular sciences · 2021Article
- Retinol-binding protein 4 mRNA translation in hepatocytes is enhanced by activation of mTORC1.American journal of physiology. Endocrinology and metabolism · 2021Article
- Diabetes enhances translation ofThe Journal of biological chemistry · 2020Article
- O-GlcNAc Transferase Inhibition Differentially Affects Breast Cancer Subtypes.Scientific reports · 2019Article
- Article
- Emerging roles of RNA-binding proteins in diabetes and their therapeutic potential in diabetic complications.Wiley interdisciplinary reviews. RNA · 2018Review
- Real Talk: The Inter-play Between the mTOR, AMPK, and Hexosamine Biosynthetic Pathways in Cell Signaling.Frontiers in endocrinology · 2018Review
- The Translational Repressor 4E-BP1 Contributes to Diabetes-Induced Visual Dysfunction.Investigative ophthalmology & visual science · 2016Article
- Regulated in development and DNA damage 1 is necessary for hyperglycemia-induced vascular endothelial growth factor expression in the retina of diabetic rodents.The Journal of biological chemistry · 2015Article
- mTORC1 and JNK coordinate phosphorylation of the p70S6K1 autoinhibitory domain in skeletal muscle following functional overloading.American journal of physiology. Endocrinology and metabolism · 2014Article
- Hyperglycemia mediates a shift from cap-dependent to cap-independent translation via a 4E-BP1-dependent mechanism.Diabetes · 2013Article
- The role of the unfolded protein response in diabetes mellitus.Seminars in immunopathology · 2013Review
- Mechanistic target of rapamycin complex 1 (mTORC1)-mediated phosphorylation is governed by competition between substrates for interaction with raptor.The Journal of biological chemistry · 2013Article
- Induction of REDD1 gene expression in the liver in response to endoplasmic reticulum stress is mediated through a PERK, eIF2α phosphorylation, ATF4-dependent cascade.Biochemical and biophysical research communications · 2012Article
- Hyperglycemia AltersIn vivo (Athens, Greece)Article
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5 authors at 1 institution in 1 country.
Funding
Abstract
4E-BP1 is a protein that, in its hypophosphorylated state, binds the mRNA cap-binding protein eIF4E and represses cap-dependent mRNA translation. By doing so, it plays a major role in the regulation of gene expression by controlling the overall rate of mRNA translation as well as the selection of mRNAs for translation. Phosphorylation of 4E-BP1 causes it to release eIF4E to function in mRNA translation. 4E-BP1 is also subject to covalent addition of N-acetylglucosamine to Ser or Thr residues (O-GlcNAcylation) as well as to truncation. In the truncated form, it is both resistant to phosphorylation and able to bind eIF4E with high affinity. In the present study, Ins2(Akita/+) diabetic mice were used to test the hypothesis that hyperglycemia and elevated flux of glucose through the hexosamine biosynthetic pathway lead to increased O-GlcNAcylation and truncation of 4E-BP1 and consequently decreased eIF4E function in the liver. The amounts of both full-length and truncated 4E-BP1 bound to eIF4E were significantly elevated in the liver of diabetic as compared with non-diabetic mice. In addition, O-GlcNAcylation of both the full-length and truncated proteins was elevated by 2.5- and 5-fold, respectively. Phlorizin treatment of diabetic mice lowered blood glucose concentrations and reduced the expression and O-GlcNAcylation of 4E-BP1. Additionally, when livers were perfused in the absence of insulin, 4E-BP1 phosphorylation in the livers of diabetic mice was normalized to the control value, yet O-GlcNAcylation and the association of 4E-BP1 with eIF4E remained elevated in the liver of diabetic mice. These findings provide insight into the pathogenesis of metabolic abnormalities associated with diabetes.
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