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Gene Review

OGT  -  O-linked N-acetylglucosamine (GlcNAc)...

Homo sapiens

Synonyms: FLJ23071, HRNT1, MGC22921, O-GLCNAC, O-GlcNAc transferase subunit p110, ...
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Disease relevance of OGT


Psychiatry related information on OGT

  • Since a greater understanding of brain OGT may provide new insights into the pathogenesis of Alzheimer's disease, we examined the characteristics and subcellular distribution of OGT protein and OGT activity and its relationship to O-linked glycosylation [6].

High impact information on OGT

  • Here, we show that O-GlcNAc transferase (OGT), the enzyme that catalyzes this posttranslational modification, interacts with a histone deacetylase complex by binding to the corepressor mSin3A [7].
  • We propose that mSin3A targets OGT to promoters to inactivate transcription factors and RNA polymerase II by O-GlcNAc modification, which acts in concert with histone deacetylation to promote gene silencing in an efficient and specific manner [7].
  • Interestingly, GmaR also functions as a glycosyltransferase exhibiting O-linked N-acetylglucosamine transferase (OGT) activity for flagellin (FlaA) [8].
  • These studies illustrate the necessity of conditional gene-targeting approaches in the mutagenesis and study of essential sex-linked genes, and indicate that OGT participation in intracellular glycosylation is essential for embryonic stem cell viability and for mouse ontogeny [9].
  • To study OGT function in vivo, we have used gene-targeting approaches in male embryonic stem cells [9].

Chemical compound and disease context of OGT

  • Several colorectal cancer cell lines express the asialoglycoprotein receptor, although no significant levels can be detected in C170HM2 cells, consistent with the observation that OGT 719 is approximately 3 log orders of magnitude less potent in vitro than 5-FU [4].
  • We expressed each of these OGT isoforms in a soluble form in Escherichia coli and have used them to identify novel targets including the Src-family tyrosine kinase yes and O-GlcNAc-ase [5].
  • When incubated with RBC suspension, OGT and its four constituting herbs provided strong protection for RBC membrane to hemolysis induced by 2,2-azo-bis (2-amidinopropane) dihydrochloride (AAPH), an azo free radical initiator [10].

Biological context of OGT

  • We find that OGT mutagenesis requires a strategy that retains an intact OGT gene as accomplished by using Cre-loxP recombination, because a deletion in the OGT gene results in loss of embryonic stem cell viability [9].
  • A single copy of the OGT gene is present in the male genome and resides on the X chromosome near the centromere in region D in the mouse spanning markers DxMit41 and DxMit95, and in humans at Xq13, a region associated with neurologic disease [9].
  • Segregation of OGT alleles in the mouse germ line with ZP3-Cre recombination in oocytes reveals that intact OGT alleles are required for completion of embryogenesis [9].
  • These studies support the model that the catalytic subunit of OGT achieves both high specificity and a remarkable diversity of substrates by complexing with a variety of targeting proteins via its TPR protein-protein interaction domains [11].
  • Identification of viable OGT mutants may facilitate examination of its role in nutrient sensing and signal transduction cascades [12].

Anatomical context of OGT

  • Unlike previously described glycosyltransferases, OGT is localized to the cytosol and nucleus [13].
  • In the present study, we examined the localization of OGT mRNA and OGT protein in the rat pancreas [14].
  • To investigate this further, we incubated H-411E liver cells with insulin (10,000 microU/ml) and quantified the subcellular distribution of O-GlcNAc transferase (OGT) and O-GlcNAc-modified Sp1 [15].
  • O-GlcNAc transferase (OGT) modifies nuclear pore proteins and transcription factors [1].
  • In the islets of Langerhans, especially in the alpha-cells, intense staining with anti-OGT antibody was observed [14].

Associations of OGT with chemical compounds


Physical interactions of OGT


Other interactions of OGT


Analytical, diagnostic and therapeutic context of OGT


  1. Functional expression of O-linked GlcNAc transferase. Domain structure and substrate specificity. Lubas, W.A., Hanover, J.A. J. Biol. Chem. (2000) [Pubmed]
  2. OGT functions as a catalytic chaperone under heat stress response: a unique defense role of OGT in hyperthermia. Sohn, K.C., Lee, K.Y., Park, J.E., Do, S.I. Biochem. Biophys. Res. Commun. (2004) [Pubmed]
  3. The role of O-linked protein glycosylation in beta-cell dysfunction. Konrad, R.J., Kudlow, J.E. Int. J. Mol. Med. (2002) [Pubmed]
  4. A novel, orally administered nucleoside analogue, OGT 719, inhibits the liver invasive growth of a human colorectal tumor, C170HM2. Rohlff, C., Watson, S.A., Morris, T.M., Skelton, L., Jackman, A.L., Page, M.J. Cancer Res. (1999) [Pubmed]
  5. Recombinant O-GlcNAc transferase isoforms: identification of O-GlcNAcase, yes tyrosine kinase, and tau as isoform-specific substrates. Lazarus, B.D., Love, D.C., Hanover, J.A. Glycobiology (2006) [Pubmed]
  6. UDP-N-acetylglucosaminyl transferase (OGT) in brain tissue: temperature sensitivity and subcellular distribution of cytosolic and nuclear enzyme. Okuyama, R., Marshall, S. J. Neurochem. (2003) [Pubmed]
  7. Recruitment of O-GlcNAc transferase to promoters by corepressor mSin3A: coupling protein O-GlcNAcylation to transcriptional repression. Yang, X., Zhang, F., Kudlow, J.E. Cell (2002) [Pubmed]
  8. A bifunctional O-GlcNAc transferase governs flagellar motility through anti-repression. Shen, A., Kamp, H.D., Gr??ndling, A., Higgins, D.E. Genes Dev. (2006) [Pubmed]
  9. The O-GlcNAc transferase gene resides on the X chromosome and is essential for embryonic stem cell viability and mouse ontogeny. Shafi, R., Iyer, S.P., Ellies, L.G., O'Donnell, N., Marek, K.W., Chui, D., Hart, G.W., Marth, J.D. Proc. Natl. Acad. Sci. U.S.A. (2000) [Pubmed]
  10. Inhibitory effects of Oren-Gedoku-To (Huanglian-Jie-Du-Tang) on free radical-induced lysis of human red blood cells. Sekiya, N., Shibahara, N., Sakakibara, I., Hattori, N., Goto, H., Terasawa, K. Phytotherapy research : PTR. (2003) [Pubmed]
  11. Roles of the tetratricopeptide repeat domain in O-GlcNAc transferase targeting and protein substrate specificity. Iyer, S.P., Hart, G.W. J. Biol. Chem. (2003) [Pubmed]
  12. Mutational analysis of the catalytic domain of O-linked N-acetylglucosaminyl transferase. Lazarus, B.D., Roos, M.D., Hanover, J.A. J. Biol. Chem. (2005) [Pubmed]
  13. Dynamic glycosylation of nuclear and cytosolic proteins. Cloning and characterization of a unique O-GlcNAc transferase with multiple tetratricopeptide repeats. Kreppel, L.K., Blomberg, M.A., Hart, G.W. J. Biol. Chem. (1997) [Pubmed]
  14. Localization of the O-linked N-acetylglucosamine transferase in rat pancreas. Akimoto, Y., Kreppel, L.K., Hirano, H., Hart, G.W. Diabetes (1999) [Pubmed]
  15. Insulin stimulates and diabetes inhibits O-linked N-acetylglucosamine transferase and O-glycosylation of Sp1. Majumdar, G., Wright, J., Markowitz, P., Martinez-Hernandez, A., Raghow, R., Solomon, S.S. Diabetes (2004) [Pubmed]
  16. Identification and cloning of a novel family of coiled-coil domain proteins that interact with O-GlcNAc transferase. Iyer, S.P., Akimoto, Y., Hart, G.W. J. Biol. Chem. (2003) [Pubmed]
  17. Ataxin-10 interacts with O-GlcNAc transferase OGT in pancreatic beta cells. Andrali, S.S., März, P., Ozcan, S. Biochem. Biophys. Res. Commun. (2005) [Pubmed]
  18. A phase I safety and pharmacokinetic study of OGT 719 in patients with liver cancer. Mok, T.S., Leung, T.W., Brown, G., Moyses, C., Chan, A.T., Yeo, W., Wong, H., Chak, K., Johnson, P. Acta oncologica (Stockholm, Sweden) (2004) [Pubmed]
  19. GLP-1 release in man after lower large bowel resection or intrarectal glucose administration. Printz, H., Reiter, S., Samadi, N., Ebrahimsade, S., Kirchner, R., Arnold, R., Göke, B. Digestion (1998) [Pubmed]
  20. Reciprocity between O-GlcNAc and O-phosphate on the carboxyl terminal domain of RNA polymerase II. Comer, F.I., Hart, G.W. Biochemistry (2001) [Pubmed]
  21. Mitochondrial and nucleocytoplasmic targeting of O-linked GlcNAc transferase. Love, D.C., Kochan, J., Cathey, R.L., Shin, S.H., Hanover, J.A., Kochran, J. J. Cell. Sci. (2003) [Pubmed]
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