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O-GlcNAcase Regulates Pluripotency States of Human Embryonic Stem Cells

ABSTRACT: In order to study which part, if any, of the EP300 phenotype is related to OGA regulation.

ORGANISM(S): Homo sapiens

PROVIDER: GSE256456 | GEO | 2024/06/26

REPOSITORIES: GEO

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O-GlcNAcase Regulates Pluripotency States of Human Embryonic Stem Cells [CUT&Tag]

Project description:In order to study the occupancy by OGA throughout the genome.

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O-GlcNAcase Regulates Pluripotency States of Human Embryonic Stem Cells [ChIP-seq]

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O-GlcNAcase regulates pluripotency states of human embryonic stem cells.

Project description: Not available

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OGA-mediated protein glycosylation regulates pluripotency states in human embryonic stem cells

Project description:In our previous study, we uncovered that OGA significantly elevated in naïve hESC. Therefore, we sought to investigate the effects of O-GlcNAc on hESC and the interconvert of both pluripotent states. Depletion of OGA, which results in global O-GlcNAcylation increased, would impair naïve hESC pluripotency but can promote naïve to primed hESC transition. In addition, we obtained the profiles of O-GlcNAcylated proteins in H9 primed hESC and H9-PXGL hESC via MS based-quantitative proteomics.

2024-08-10 | PXD041605 | Pride

O-GlcNAcase is an epigenetic regulator of nutrient-responsive Drosophila Oogenesis

Project description:Nutrient-responsive oogenesis in Drosophila is a complex and dynamic process regulated, in part, by members of the Pc and Trx complexes. The recent finding that O-GlcNAc Transferase (ogt/sxc) is essential for Pc repression raises the question of whether this nutrient-sensing pathway plays a role in regulating oogenesis. OGT transfers O-GlcNAc to key transcriptional regulators in response to graded levels of the nutrient-derived precursor UDP-GlcNAc; O-GlcNAcase (OGA) catalyzes the removal of O-GlcNAc. Here we produced a null allele of oga (oga1) in Drosophila to examine its in vivo function. We found that oga mutant flies were viable, but that females displayed greatly reduced fecundity. The ovaries from the female OGA knockout exhibited a starvation-like phenotype, even under well-fed conditions. Germline stem cell division was slowed in the germarium of OGA knockout fly ovarioles. Ovaries from the oga1 mutants displayed significantly decreased H3K4 monomethylation in germline stem cells. The Trithorax family members Trx and Ash1 and Compass member Set1 histone methyltransferases are O-GlcNAc modified in oga1 mutant ovaries. Our results suggest that the loss of OGA disrupts oogenesis at least in part by interfering with H3K4 monomethylation in germ cells in the ovary. The findings also suggest that O-GlcNAc cycling is an essential part of the nutrient-responsive epigenetic machinery regulating Drosophila oogenesis in response to a changing nutrient supply.

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Effects of O-GlcNAc modification on gene expression using O-GlcNAcase deleted Mouse Embryonic Fibroblast cells.

Project description:Single O-GlcNAc modification orchestrate by O-GlcNAc Transferase (OGT) and O-GlcNAcase (OGA alias MGEA5) enzymes, affects signal transduction and gene expression by chromatin modulation. We developed Oga deleted MEF (mouse embryonic fibroblast) cells to investigate effects of O-GlcNAc modification in mice. RNA isolated from Mouse Embryonic Fibroblast cells generated from Oga Knock out (KO) Heterozygous (Het) and wild type (WT) cells and subjected to microarray analysis. Results provide insight into regulatory pattern of O-GlcNAc modification, and associated signaling pathways

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O-GlcNAcase Regulates Pluripotency States of Human Embryonic Stem Cells

Project description:O-GlcNAcase Regulates Pluripotency States of Human Embryonic Stem Cells

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O-GlcNAcase Regulates Pluripotency States of Human Embryonic Stem Cells [ChIP-seq]

Project description:O-GlcNAcase Regulates Pluripotency States of Human Embryonic Stem Cells [ChIP-seq]

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O-GlcNAcase Regulates Pluripotency States of Human Embryonic Stem Cells [CUT&Tag]

Project description:O-GlcNAcase Regulates Pluripotency States of Human Embryonic Stem Cells [CUT&Tag]

| PRJNA1082670 | ENA

Stress-induced interactome of the O-GlcNAcase by SILAC-BioID-MS/MS

Project description:O-linked-β-N-acetylglucosamine (O-GlcNAc) dynamically modifies and regulates thousands of nuclear, cytoplasmic, and mitochondrial proteins. Cellular stress, including oxidative stress, results in increased O-GlcNAcylation on numerous proteins and this is thought to promote cell survival. The mechanisms by which the O-GlcNAc transferase (OGT) and the O-GlcNAcase (OGA), the enzymes that add and remove O-GlcNAc respectively, are regulated leading to oxidative stress-induced changes in O-GlcNAcylation are not fully characterized. Here, we demonstrate that oxidative stress leads to elevated O-GlcNAc levels in U2OS cells, but has little impact on the activity of OGT. In contrast, the expression and activity of OGA are enhanced. We hypothesized that protein interactors of OGA may control the local activity or substrate targeting of this enzyme, resulting in stress-induced elevations of O-GlcNAc. We utilized the BioID proximity biotinylation technique in combination with Stable Isotope Labeling of Amino Acids in Cell culture (SILAC) to define the basal and oxidative stress-dependent interactomes of OGA. Our study revealed 90 OGA-interacting partners, many of which exhibit increased binding upon oxidative stress. The associations of OGA with fatty acid synthase (FAS), filamin-A, heat shock cognate 70 kDa protein, and OGT were confirmed by co-immunoprecipitation. The pool of OGA bound to FAS demonstrates a substantial (~85%) reduction in catalytic activity, suggesting that FAS is an inhibitor of OGA. Consistent with this observation, FAS overexpression augments stress-induced O-GlcNAcylation. Together, these data suggest that O-GlcNAcylation may be one downstream effector of FAS that fine-tunes the cell’s response to stress and injury.

2017-03-14 | PXD005039 | Pride

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