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Nutrient sensing mediated by O-GlcNAcylation regulates gene expression through epigenetic mechanisms during embryonic neurogenesis

ABSTRACT: Nutrient sensing mediated by O-GlcNAcylation regulates gene expression through epigenetic mechanisms during embryonic neurogenesis

PROVIDER: PRJNA717264 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR14071045_1.fastq.gz	Fastqsanger.gz
	SRR14071045_2.fastq.gz	Fastqsanger.gz
	SRR14071046_1.fastq.gz	Fastqsanger.gz
	SRR14071046_2.fastq.gz	Fastqsanger.gz
	SRR14071047_1.fastq.gz	Fastqsanger.gz

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Similar Datasets

Nutrient sensing mediated by O-GlcNAcylation regulates gene expression through epigenetic mechanisms during embryonic neurogenesis

Project description:We show that pharmacological upregulation of O-GlcNAc levels during hESCs-neuronal differentiation leads to upregulation of key neurogenic TF gene which in turn is associated with increased H3K4me3 levels, reduction in H3K27me3 levels and increase in Pol IISer5 phosphorylation. Our results demonstrate O-GlcNAc mediated sensitivity of chromatin to nutrient status, and indicate how metabolic dysregulations could affect stem cell fate decisions through epigenetic gene regulatory mechanisms

2022-03-26 | GSE169649 | GEO

Nutrient Responsive O-GlcNAcylation Dynamically Modulates Galectin 3 Secretion

Project description:Endomembrane glycosylation and cytoplasmic O-GlcNAcylation each play essential roles in nutrient sensing, and in fact, characteristic changes in glycan patterns have been described in disease states such as diabetes and cancer. These changes in glycosylation have important functional roles and can drive disease progression. However, little is known about the molecular mechanisms underlying how these signals are integrated and transduced into biological effects. Galectins are proteins that bind glycans and are secreted by a poorly characterized non-classical secretory mechanism. Once outside the cell, galectins bind to terminal galactose residues of cell surface glycans and modulate numerous extracellular functions like clathrin independent endocytosis (CIE). Originating in the cytoplasm, galectins are predicted substrates for O-GlcNAc addition and removal; and, as we have shown, galectin 3 is a substrate for OGT. This study also shows that galectin 3 secretion is sensitive to changes in O-GlcNAc levels. We determined that there is a significant difference in O-GlcNAcylation status between cytoplasmic and secreted galectin 3. We observed dramatic alterations in galectin 3 secretion in response to nutrient conditions and these changes were dependent on dynamic O-GlcNAcylation. Importantly, we showed that these O-GlcNAc driven alterations in galectin 3 secretion drove changes in CIE. These results indicate that dynamic O-GlcNAcylation of galectin 3 plays a role in modulating its secretion and can tune its function of transducing nutrient sensing information coded in cell surface glycosylation into biological effects.

2022-04-01 | PXD028139 | Pride

Nutrient sensitive protein <i>O</i>-GlcNAcylation modulates the transcriptome through epigenetic mechanisms during embryonic neurogenesis.

Project description:Protein O-GlcNAcylation is a dynamic, nutrient-sensitive mono-glycosylation deposited on numerous nucleo-cytoplasmic and mitochondrial proteins, including transcription factors, epigenetic regulators, and histones. However, the role of protein O-GlcNAcylation on epigenome regulation in response to nutrient perturbations during development is not well understood. Herein we recapitulated early human embryonic neurogenesis in cell culture and found that pharmacological up-regulation of O-GlcNAc levels during human embryonic stem cells' neuronal differentiation leads to up-regulation of key neurogenic transcription factor genes. This transcriptional de-repression is associated with reduced H3K27me3 and increased H3K4me3 levels on the promoters of these genes, perturbing promoter bivalency possibly through increased EZH2-Thr311 phosphorylation. Elevated O-GlcNAc levels also lead to increased Pol II-Ser5 phosphorylation and affect H2BS112O-GlcNAc and H2BK120Ub1 on promoters. Using an in vivo rat model of maternal hyperglycemia, we show similarly elevated O-GlcNAc levels and epigenetic dysregulations in the developing embryo brains because of hyperglycemia, whereas pharmacological inhibition of O-GlcNAc transferase (OGT) restored these molecular changes. Together, our results demonstrate O-GlcNAc mediated sensitivity of chromatin to nutrient status, and indicate how metabolic perturbations could affect gene expression during neurodevelopment.

| S-EPMC9039347 | biostudies-literature

Regulation of NRF2 signaling by O-GlcNAcylation of KEAP1

Project description:O-GlcNAcylation is an essential, nutrient-sensitive post-translational modification, but its biochemical and phenotypic effects remain incompletely understood. To address this knowledge gap, we investigated the global transcriptional response to perturbations in O-GlcNAcylation. Unexpectedly, many transcriptional effects of O-GlcNAc transferase (OGT) inhibition were due to the activation of NRF2, the master regulator of redox stress tolerance. Moreover, we found that a signature of low OGT activity strongly correlates with NRF2 activation in multiple tumor expression datasets. Guided by this information, we identified KEAP1 (also known as KLHL19), the primary negative regulator of NRF2, as a direct substrate of OGT. We show that O-GlcNAcylation of KEAP1 at serine 104 is required for the efficient ubiquitination and degradation of NRF2. Interestingly, O-GlcNAc levels and NRF2 activation co-vary in response to glucose fluctuations, indicating that KEAP1 O-GlcNAcylation links nutrient sensing to downstream stress resistance. Our results reveal a novel regulatory connection between nutrient-sensitive glycosylation and NRF2 signaling, and provide a blueprint for future approaches to discover functionally important O-GlcNAcylation events on other KLHL family proteins in various experimental and disease contexts.

2017-06-26 | GSE81740 | GEO

Ceramide-FGF13 axis regulate nutrient sensing

Project description:Ceramide-FGF13 axis regulate nutrient sensing

| PRJNA997260 | ENA

Nutrient sensing modulates malaria parasite virulence.

Project description:Nutrient sensing modulates malaria parasite virulence.

| PRJNA286025 | ENA

Chaperone dependent coordination of nutrient sensing and energy metabolism by mTORC2

Project description:mTORC2 senses nutrients and coordinates substrate metabolism and macromolecule synthesis program with the availability of external nutrient availability. Knockdown of mTORC2 components and its chaperone partners impairs both nutrient sensing and downstrem metabolism/growth programs.

2020-01-23 | GSE93948 | GEO

O-GlcNAcylation of human TATA-Box binding protein is required to sustain key metabolic enzyme gene expression

Project description:Cellular homeostasis is ensured by myriad cellular processes that integrate environmental changes and maintain stability within the organism. Variation in nutrient availability can be reflected by the post-translational modification of many proteins by the nutrient sensor O-GlcNAcylation. Herein, we describe a molecular mechanism of transcription regulation by O-GlcNAcylation of the TATA-box binding protein (TBP). We show that O-GlcNAcylation regulates its interaction with BTAF1, hence, formation of the B-TFIID complex, and its dynamic cycling on and off of DNA. We mapped three O-GlcNAcylation sites at the N-terminus of TBP and defined T114 as a main regulator of the interaction with BTAF1. CRISPR/Cas9 editing of wild-type TBP replaced by a T114A mutant, leads to profound modification of HeLa cells’ glucose and lipid metabolism and gene expression profile. These data indicate that basal transcription machinery, via O-GlcNAcylation of TBP, can integrate nutrient availability and modulate the transcriptome, resulting in adaptation of cellular metabolism.

2020-04-14 | GSE106231 | GEO

GlcNAcylation of histone H2B facilitates its monoubiquitination

Project description:This SuperSeries is composed of the following subset Series: GSE33049: GlcNAcylation of histone H2B facilitates its monoubiquitination [Illumina Genome Analyzer data] GSE33050: GlcNAcylation of histone H2B facilitates its monoubiquitination [Affymetrix data] Refer to individual Series

2011-10-26 | E-GEOD-33051 | biostudies-arrayexpress

Stem cell intrinsic nutrient sensing regulating diet dependent intestinal adaptation

Project description:The intestine is an organ with exceptionally high rate of cell turnover and perturbations in this process can lead to disease such as cancer or intestinal atrophy. Nutrition is a key factor regulating the intestinal cell turnover and has a profound impact on intestinal volume and cellular architecture. However, how the intestinal equilibrium is maintained in fluctuating dietary conditions is insufficiently understood. By utilizing the Drosophila midgut as a model, we reveal a novel nutrient sensing mechanism coupling stem cell metabolism with stem cell extrinsic growth signal. Our results show that intestinal stem cells (ISCs) employ the hexosamine biosynthesis pathway (HBP) to monitor nutritional status and energy metabolism. Elevated activity of the HBP promotes Warburg effect-like metabolic reprogramming, which is required for the reactivation of ISCs from calorie restriction-induced quiescence. Furthermore, the HBP activity is an essential facilitator for insulin signaling-induced intestinal growth. In conclusion, intestinal stem cell intrinsic nutrient sensing regulates metabolic pathway activities, and defines the stem cell responsiveness to niche-derived growth signals.

2018-09-13 | GSE107052 | GEO

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