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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

O-linked N-acetylglucosamine

OGT, O-linked GlcNAc transferase
This gene encodes a glycosyltransferase that catalyzes the addition of a single N-acetylglucosamine in O-glycosidic linkage to serine or threonine residues. Since both phosphorylation and glycosylation compete for similar serine or threonine residues, the two processes may compete for sites, or they may alter the substrate specificity of nearby sites by steric or electrostatic effects. The protein contains multiple tetratricopeptide repeats that are required for optimal recognition of substrates. Alternatively spliced transcript variants encoding distinct isoforms have been found for this gene. [provided by RefSeq, Oct 2009] (from NCBI)
Top mentioned proteins: CAN, V1a, Insulin, ACID, HAD
Papers using OGT antibodies
Murine platelets are not regulated by O-linked beta-N-acetylglucosamine
Planel Emmanuel, In PLoS ONE, 2007
... OGTSigma Aldrich, St ...
AMPK activation as a strategy for reversing the endothelial lipotoxicity underlying the increased vascular risk associated with insulin resistance syndrome.
Xu Aimin, In PLoS ONE, 2004
... Anti-O-GlcNAc antibody (CTD110.6 antibody, sc-59623) and negative control siRNA or target-specific siRNA duplex against OGT were from Santa Cruz Biotechnology (Santa Cruz, CA) ...
Papers on OGT
O-GlcNAcylation of master growth repressor DELLA by SECRET AGENT modulates multiple signaling pathways in Arabidopsis.
Sun et al., Durham, United States. In Genes Dev, Feb 2016
Here, we show that DELLAs are modified by the O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT) SECRET AGENT (SEC) in Arabidopsis.
Visualization of Protein-Specific Glycosylation inside Living Cells.
Wittmann et al., Konstanz, Germany. In Angew Chem Int Ed Engl, Feb 2016
Herein, we demonstrate protein-specific detection of the glycosylation of the intracellular proteins OGT, Foxo1, p53, and Akt1 in living cells.
Dexamethasone-Induced Skeletal Muscle Atrophy Increases O-GlcNAcylation in C2C12 Cells.
Papini et al., Milano, Italy. In J Cell Biochem, Feb 2016
O-GlcNAcylation, a regulatory post-translational modification of nuclear and cytoplasmic proteins consists in the attachment of O-GlcNAc residues on cell proteins and is regulated by two enzymes: O-GlcNAc-transferase (OGT) and O-GlcNAcase (OGA).
Differential membranous E-cadherin expression, cell proliferation and O-GlcNAcylation between primary and metastatic nodal lesion in colorectal cancer.
Jang, South Korea. In Pathol Res Pract, Jan 2016
Primary CRC showed higher expression of O-GlcNAcylation and O-GlcNAc-transferase (OGT) than nonneoplastic colons.
Intracellular and extracellular O-linked N-acetylglucosamine in the nervous system.
Okajima et al., Nagoya, Japan. In Exp Neurol, Dec 2015
Addition of O-linked N-acetylglucosamine (O-GlcNAc) to the hydroxyl group of serine and threonine residues (O-GlcNAcylation) is a post-translational modification common to multicellular eukaryotes.
A critical perspective of the diverse roles of O-GlcNAc transferase in chromatin.
Müller et al., Martinsried, Germany. In Chromosoma, Dec 2015
O-linked β-N-Acetylglucosamine (O-GlcNAc) is a posttranslational modification that is catalyzed by O-GlcNAc transferase (Ogt) and found on a plethora of nuclear and cytosolic proteins in animals and plants.
Glucose Alters Per2 Rhythmicity Independent of AMPK, Whereas AMPK Inhibitor Compound C Causes Profound Repression of Clock Genes and AgRP in mHypoE-37 Hypothalamic Neurons.
Belsham et al., Toronto, Canada. In Plos One, Dec 2015
Thus, the AMPK inhibitor Compound C was utilized, and mRNA levels of Per2, Bmal1, Cryptochrome1 (Cry1), agouti-related peptide (AgRP), carnitine palmitoyltransferase 1C (Cpt1c), and O-linked N-acetylglucosamine transferase (Ogt) were measured.
The omniscient placenta: Metabolic and epigenetic regulation of fetal programming.
Bale et al., Philadelphia, United States. In Front Neuroendocrinol, Oct 2015
The X-linked enzyme O-linked-N-acetylglucosamine transferase (OGT) acts as a nutrient sensor that modifies numerous proteins to alter various cellular signals, including major epigenetic processes.
You are what you eat: O-linked N-acetylglucosamine in disease, development and epigenetics.
Hanover et al., Bethesda, United States. In Curr Opin Clin Nutr Metab Care, Jul 2015
PURPOSE OF REVIEW: The O-linked N-acetylglucosamine (O-GlcNAc) modification is both responsive to nutrient availability and capable of altering intracellular cellular signalling.
O-GlcNAc-modification of SNAP-29 regulates autophagosome maturation.
Zhang et al., Beijing, China. In Nat Cell Biol, 2014
Here, we report that O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT) mediates O-GlcNAcylation of the SNARE protein SNAP-29 and regulates autophagy in a nutrient-dependent manner.
TET proteins and epigenetic modifications in cancers.
Krześlak et al., Łódź, Poland. In Postepy Hig Med Dosw (online), 2014
EZH2, OGT, Sin3a or HCF1) and by affecting their activity and, chromatin binding ability, they can cause changes in patterns of histone methylation, acetylation and O-GlcNAcylation.
O-GlcNAc transferase enables AgRP neurons to suppress browning of white fat.
Yang et al., New Haven, United States. In Cell, 2014
The levels of O-GlcNAc transferase (OGT) and O-GlcNAc modification are enriched in AgRP neurons and are elevated by fasting.
O-GlcNAc and neurodegeneration: biochemical mechanisms and potential roles in Alzheimer's disease and beyond.
Vocadlo et al., Canada. In Chem Soc Rev, 2014
One such process of interest is the addition of O-linked N-acetylglucosamine (O-GlcNAc) residues onto nuclear and cytoplasmic proteins within mammals.
Glucose regulates mitochondrial motility via Milton modification by O-GlcNAc transferase.
Schwarz et al., Boston, United States. In Cell, 2014
Here, we report a molecular mechanism by which nutrient availability in the form of extracellular glucose and the enzyme O-GlcNAc Transferase (OGT), whose activity depends on glucose availability, regulates mitochondrial motility in neurons.
HCF-1 is cleaved in the active site of O-GlcNAc transferase.
Walker et al., Boston, United States. In Science, 2014
Host cell factor-1 (HCF-1), a transcriptional co-regulator of human cell-cycle progression, undergoes proteolytic maturation in which any of six repeated sequences is cleaved by the nutrient-responsive glycosyltransferase, O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT).
Hsp90 regulates O-linked β-N-acetylglucosamine transferase: a novel mechanism of modulation of protein O-linked β-N-acetylglucosamine modification in endothelial cells.
Catravas et al., Augusta, United States. In Am J Physiol Cell Physiol, 2012
Hsp90 is involved in the regulation of OGT and O-GlcNAc modification and that Hsp90 inhibitors might be used to modulate O-GlcNAc modification and reverse its adverse effects in human diseases.
O-GlcNAc transferase is involved in glucocorticoid receptor-mediated transrepression.
Yang et al., New Haven, United States. In J Biol Chem, 2012
These studies identify a molecular mechanism of GR transrepression, and highlight the function of O-GlcNAc in hormone signaling.
Expression of genes encoding for enzymes associated with O-GlcNAcylation in endometrial carcinomas: clinicopathologic correlations.
Bryś et al., Łódź, Poland. In Ginekol Pol, 2012
O-GlcNAcylation may be an important regulatory modification involved in endometrial cancer pathogenesis but the actual significance of this modification for endometrial cancer progression needs to be investigated further.
Regulation of the proteasome by AMPK in endothelial cells: the role of O-GlcNAc transferase (OGT).
Zou et al., Oklahoma City, United States. In Plos One, 2011
AMPK functions as a physiological suppressor of 26S proteasomes through OGT
Prediction of bladder cancer based on urinary content of MGEA5 and OGT mRNA level.
Lipinski et al., Łódź, Poland. In Clin Lab, 2011
Analysis of urinary content of MGEA5 and OGT may be useful for bladder cancer diagnostics.
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