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Here is presented a novel O-GlcNAc transferase (OGT), EOGT, responsible for extracellular O-linked-N-acetylglucosamine acylation.
study found that the super sex combs (sxc)gene encodes O-linked N-acetylglucosamine transferase (Ogt); Polycomb repression appears to be a critical function of Sxc/Ogt in Drosophila and may be mediated by the glycosylation of Polyhomeotic
We identify a TET1 domain that is necessary and sufficient for binding to OGT and report a point mutation that disrupts the TET1-OGT interaction.show that this interaction is necessary for TET1 to rescue hematopoetic stem cell production in tet mutant zebrafish embryos, suggesting that OGT promotes TET1's function during development.
Developmental regulation of zOGT transcriptional variants generated by alternative splicing and characterization of their OGT activities of protein O-GlcNAcylation.
Overexpression of Ogt delayed epiboly and caused a severe disorganization of the microtubule and actin based cytoskeleton in the extra-embryonic yolk syncytial layer.
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.
miR-483 inhibited the expression level of OGT mRNA by direct binding to its 3'-untranslated region. Expression of miR-483 was negatively correlated with OGT in gastric cancer tissues.
novel regulatory mechanism for O-GlcNAcylation during FA complex formation, which thereby affects integrin activation and integrin-mediated functions such as cell adhesion and migration
a novel ASXL1-OGT axis and raise the possibility that this axis has a tumor-suppressor role in myeloid malignancies.
The intellectual disability L254F mutation in OGT affects activity. The L254F mutation leads to shifts up to 12 A in the OGT structure. Thermal denaturing studies reveal reduction in tetratricopeptide repeat domain stability caused by L254F. L254F OGT mutation leads to conformational changes of the tetratricopeptide repeats and reduced activity, revealing the molecular mechanisms contributing to pathogenesis.
O-GlcNAcylation and the expression of O-linked-beta-N-acetylglucosamine transferase (OGT) were upregulated in bladder cancer cell lines and tissue specimens.
High OGT expression promotes cancer lipid metabolism via SREBP-1 regulation.
O-GlcNAc transferase missense mutations is associated with X-linked intellectual disability.
The O-GlcNAc transferase OGT interacts with and post-translationally modifies the transcription factor HOXA1.
These data predict that under conditions where O-GlcNAc levels are high (breast cancer) progesterone receptor (PR) through an interaction with the modifying enzyme OGT, will exhibit increased O-GlcNAcylation and potentiated transcriptional activity. Therapeutic strategies aimed at altering cellular O-GlcNAc levels may have profound effects on PR transcriptional activity in breast cancer
Study found that levels of placental Ogt determine sex differences in fetally derived placental trophoblast transcriptome profiles associated with key developmental processes and shape genome-wide patterning of the ubiquitous epigenetic transcriptional repressive mark, H3K27me3.
High OGT expression is associated with breast cancer.
O-GlcNAc transferase (OGT) is a partner of the MCM2-7 complex and O-GlcNAcylation might regulate MCM2-7 complex by regulating the chromatin loading of MCM6 and MCM7 and stabilizing MCM/MCM interactions.
LXRalpha interacts with OGT in its N-terminal domain and ligand-binding domain (LBD) in a ligand-independent fashion.
Findings demonstrate a novel role of Poleta O-GlcNAcylation by OGT in translesion DNA synthesis regulation and genome stability maintenance.
OGT, a unique glycosyltransferase enzyme, was identified to be upregulated in non-alcoholic fatty liver disease-associated hepatocellular carcinoma tissues by transcriptome sequencing. Here, we found that OGT plays a role in cancer by promoting tumor growth and metastasis in cell models. This effect is mediated by the induction of palmitic acid.
Nrf1 is regulated by O-GlcNAc transferase.
Findings indicate O-linked N-acetylglucosamine transferase (OGT) as a cellular factor involved in human papillomaviruses type 16/18 E6 and E7 expressions and cervical cancer tumorigenesis, suggesting that targeting OGT in cervical cancer may have potential therapeutic benefit.
The findings suggest that OGT promotes the O-GlcNAc modification of HDAC1 in the development of progression hepatocellular carcinoma.
Tax interacts with the host OGT/OGA complex and inhibits the activity of OGT-bound OGA.
We identified two human PRC2 complexes and two PR-DUB deubiquitination complexes, which contain the O-linked N-acetylglucosamine transferase OGT1 and several transcription factors.
Data suggest that enzymes in hexosamine biosynthesis pathway and downstream protein O-GlcNAcylation are important for preimplantation development; these include Ogt, Gfpt (glutamine-fructose-6-P aminotransferase), and Oga (O-GlcNAcase).
Muscle-specific OGT knockout mice were lean, with increased body energy expenditure and insulin sensitivity. OGT in muscle mediates transcriptional repression of Il15 by O-GlcNAcylating EZH2.
Ogt is not only important for triggering B cell receptor-mediated signaling pathways, but also for the survival of mature, germinal center B cells.
Data show that postsynaptic deletion of O-GlcNAc transferase (OGT) leads to fewer morphological synapses.
miR-24-1 may regulate mouse hepatocarcinoma cells migration and invasion, at least partially through targeting OGT.
O-GlcNAc modification is essential for cold-induced thermogenesis and mitochondrial biogenesis in brown adipose tissue.
This work uncovers that URI-regulated OGT confers c-MYC-dependent survival functions in response to glucose fluctuations.
This study identifies OGT activity as an important regulator of SC functions such as myelin maintenance and axonal support.
cullin 3 (CUL3), a cullin family E3 ubiquitin ligase, down-regulates the expression of the O-GlcNAc transferase (OGT) and inhibits STAT3 O-GlcNAcylation.
OGT functions in metastatic spread of HPV E6/E7-positive tumor cells to the lungs through E6/E7, HCF-1 and CXCR4
Furthermore, both Ogt and Oga were required for the reversion from primed ESD-EpiSCs to naive rESCs. These findings indicate that O-GlcNAcylation plays an important role in the survival of primed ESD-EpiSCs and in their reversion to naive rESCs.
Beyond its well-known role in adding beta-O-GlcNAc to serine and threonine residues of nuclear and cytoplasmic proteins, OGT also acts as a protease in the maturation of the cell cycle regulator, HCF-1, and serves as an integral member of several protein complexes, many of them linked to gene expression. (Review)
the O-linked N-acetylglucosamine (O-GlcNAc) processing enzymes, O-GlcNAc-transferase (OGT) and O-GlcNAcase (OGA), interact with the (A)gamma-globin promoter at the -566 GATA repressor site
OGT overexpression increased the level of OGA, suggesting a compensatory mechanism for the aberrant O-GlcNAcylation.
O-GlcNAc transferase is at least partially required for maintaining cellular proliferative and migratory capacities of cardiomyocytes
E2F1 negatively regulates both Ogt and Mgea5 expression in an Rb1 protein-dependent manner.
The hyperphagia derived from the paraventricular nucleus of the hypothalamus, where loss of OGT was associated with impaired satiety.
26S proteasome-mediated OGT reduction contributed to hypoxia-induced vascular endothelial inflammatory response.
Glucosamine-induced OGT activation mediates glucose production through cleaved Notch1 and FoxO1, which contributes to the regulation of maintenance of self-renewal in mouse embryonic stem cells.
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.
O-linked N-acetylglucosamine (GlcNAc) transferase (UDP-N-acetylglucosamine:polypeptide-N-acetylglucosaminyl transferase)
, O-linked GlcNAc transferase
, UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase
, O-linked N-acetylglucosamine transferase
, lethal (2) NC130
, O-linked N-acetylglucosamine (GlcNAc) transferase (UDP-N-acetylglucosamine:polypeptide-N-acetylglucosaminyl transferase) 1
, copy I
, UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
, o-linked GlcNAc transferase
, TPR repeat-containing protein
, UDP-N-acetylglucosamine:peptide N-acetylglucosaminyltransferase
, O linked N-acetylglucosamine transferase
, O-GlcNAc transferase subunit p110
, O-linked N-acetylglucosamine transferase 110 kDa subunit
, UDP-N-acetylglucosamine:polypeptide-N-acetylglucosaminyl transferase
, O-GlcNAc transferase p110 subunit
, uridinediphospho-N-acetylglucosamine:polypeptide beta-N-acetylglucosaminyl transferase
, O linked N-acetylglucosamine transferase like