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    Ogt O-linked N-acetylglucosamine (GlcNAc) transferase [ Rattus norvegicus (Norway rat) ]

    Gene ID: 26295, updated on 27-Nov-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    These findings indicate that oxidative environment promotes O-GlcNAcylation in skeletal muscle and suggest an interrelationship between cellular redox state and O-GlcNAc protein modificatio

    Glutathione depletion and acute exercise increase O-GlcNAc protein modification in rat skeletal muscle.
    Peternelj TT, Marsh SA, Strobel NA, Matsumoto A, Briskey D, Dalbo VJ, Tucker PS, Coombes JS.

    09/26/2015
    Findings suggest that, by dynamically regulating Milton GlcNAcylation, OGT tailors mitochondrial dynamics in neurons based on nutrient availability.

    Glucose regulates mitochondrial motility via Milton modification by O-GlcNAc transferase.
    Pekkurnaz G, Trinidad JC, Wang X, Kong D, Schwarz TL., Free PMC Article

    09/20/2014
    protein O-GlcNAcylation, OGT, and OGA in the rat brain at various ages from embryonic day 15 to the age of 2 years

    Developmental regulation of protein O-GlcNAcylation, O-GlcNAc transferase, and O-GlcNAcase in mammalian brain.
    Liu Y, Li X, Yu Y, Shi J, Liang Z, Run X, Li Y, Dai CL, Grundke-Iqbal I, Iqbal K, Liu F, Gong CX., Free PMC Article

    02/2/2013
    results suggest that cultured podocytes possess limited ability to synthesize glucosamine (GlcN) internally and therefore may need to receive GlcN from the extracellular environment.

    Expression of GFAT1 and OGT in podocytes: transport of glucosamine and the implications for glucose uptake into these cells.
    Rogacka D, Piwkowska A, Jankowski M, Kocbuch K, Dominiczak MH, Stepiński JK, Angielski S.

    10/23/2010
    Exerts pro-survival actions during hypoxia-reoxygenation in cardiac myocytes, particularly at the level of mitochondria.

    Non-canonical glycosyltransferase modulates post-hypoxic cardiac myocyte death and mitochondrial permeability transition.
    Ngoh GA, Watson LJ, Facundo HT, Dillmann W, Jones SP., Free PMC Article

    01/21/2010
    CaMKIV activates OGT (o-linked GlcNAc transferase), and OGT has an essential role on the process of CaMKIV-dependent AP-1 activation under depolarization in neuronal cells.

    o-GlcNAc transferase is activated by CaMKIV-dependent phosphorylation under potassium chloride-induced depolarization in NG-108-15 cells.
    Song M, Kim HS, Park JM, Kim SH, Kim IH, Ryu SH, Suh PG.

    01/21/2010
    These data support the notion that O-GlcNAc may play an important role as an internal stress response and that glucosamine-induced cardioprotection may be mediated via the p38 MAPK pathway.

    Glucosamine cardioprotection in perfused rat hearts associated with increased O-linked N-acetylglucosamine protein modification and altered p38 activation.
    Fülöp N, Zhang Z, Marchase RB, Chatham JC., Free PMC Article

    01/21/2010
    O-GlcNAc transferase binds to protein phosphatase 1 catalytic subunits

    O-GlcNAc transferase is in a functional complex with protein phosphatase 1 catalytic subunits.
    Wells L, Kreppel LK, Comer FI, Wadzinski BE, Hart GW.

    01/21/2010
    Neurodegenerative disease protein ataxin-10 (Atx-10) is associated with cytoplasmic O-linked beta-N-acetylglucosamine transferase in in the brain

    Ataxin-10 interacts with O-linked beta-N-acetylglucosamine transferase in the brain.
    März P, Stetefeld J, Bendfeldt K, Nitsch C, Reinstein J, Shoeman RL, Dimitriades-Schmutz B, Schwager M, Leiser D, Ozcan S, Otten U, Ozbek S.

    01/21/2010
    Purification of a glycosylated protein p135, and it's identification as a O-GlcNAc transferase

    Purification of the O-glycosylated protein p135 and identification as O-GlcNAc transferase.
    Konrad RJ, Tolar JF, Hale JE, Knierman MD, Becker GW, Kudlow JE.

    01/21/2010
    The 26S proteasome can be inhibited by modification with the enzyme, O-GlcNAc transferase (OGT), thus inhibiting the proteolysis of transcription factor Sp1 and a hydrophobic peptide through inhibition of ATPase activity.

    O-GlcNAc modification is an endogenous inhibitor of the proteasome.
    Zhang F, Su K, Yang X, Bowe DB, Paterson AJ, Kudlow JE.

    01/21/2010
    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 tetratricopeptide repeat protein-protein interaction domains

    Roles of the tetratricopeptide repeat domain in O-GlcNAc transferase targeting and protein substrate specificity.
    Iyer SP, Hart GW.

    01/21/2010
    examined the characteristics and subcellular distribution of OGT protein and OGT activity and relationship to O-linked glycosylation; cytosolic OGT activity is 10 times more abundant in brain tissue compared with muscle, adipose, heart, and liver

    UDP-N-acetylglucosaminyl transferase (OGT) in brain tissue: temperature sensitivity and subcellular distribution of cytosolic and nuclear enzyme.
    Okuyama R, Marshall S.

    01/21/2010
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