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STAT3S727 Phosphorylation in VTA Dopaminergic Neurons Competed by O-GlcNAcylation Regulates Acute Stress-Induced Anxiety and Reward Inhibition [RNA-Seq Ogt]

ABSTRACT: STAT3S727 Phosphorylation in VTA Dopaminergic Neurons Competed by O-GlcNAcylation Regulates Acute Stress-Induced Anxiety and Reward Inhibition [RNA-Seq Ogt]

PROVIDER: PRJNA1155652 | ENA |

REPOSITORIES: ENA

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STAT3S727 Phosphorylation in VTA Dopaminergic Neurons Competed by O-GlcNAcylation Regulates Acute Stress-Induced Anxiety and Reward Inhibition [RNA-Seq Ogt]

Project description:Acute stress can inhibit the activity of dopaminergic neurons in the ventral tegmental area (VTA), leading to increased anxiety and reduced sensitivity to natural rewards. However, the molecular mechanisms underlying this effect remain unclear. Our study shows that acute restraint stress increases the phosphorylation of the transcription factor STAT3 at Ser727 and Tyr705 in VTA dopaminergic neurons, enhancing its transcriptional activity. This modulation contributes to the inhibition of dopaminergic neuron activity, heightened anxiety, and reduced reward sensitivity. Furthermore, acute stress also promotes O-GlcNAcylation in VTA neurons, which competes with STAT3 Ser727 but not Tyr705 phosphorylation and modulates its transcriptional activity, leading to alterations in GABA receptor expression. This reveals a complex molecular feedback mechanism where O-GlcNAcylation regulates STAT3 activity to maintain brain homeostasis during acute stress responses.

2025-09-01 | GSE276183 | GEO

STAT3S727 Phosphorylation in VTA Dopaminergic Neurons Competed by O-GlcNAcylation Regulates Acute Stress-Induced Anxiety and Reward Inhibition [ATAC-Seq]

2025-09-01 | GSE276171 | GEO

STAT3S727 Phosphorylation in VTA Dopaminergic Neurons Competed by O-GlcNAcylation Regulates Acute Stress-Induced Anxiety and Reward Inhibition [RNA-Seq stress]

2025-09-01 | GSE276173 | GEO

STAT3S727 Phosphorylation in VTA Dopaminergic Neurons Competed by O-GlcNAcylation Regulates Acute Stress-Induced Anxiety and Reward Inhibition

2024-09-07 | PXD055720 |

STAT3S727 Phosphorylation in VTA Dopaminergic Neurons Competed by O-GlcNAcylation Regulates Acute Stress-Induced Anxiety and Reward Inhibition [ATAC-Seq]

Project description:STAT3S727 Phosphorylation in VTA Dopaminergic Neurons Competed by O-GlcNAcylation Regulates Acute Stress-Induced Anxiety and Reward Inhibition [ATAC-Seq]

| PRJNA1155620 | ENA

STAT3S727 Phosphorylation in VTA Dopaminergic Neurons Competed by O-GlcNAcylation Regulates Acute Stress-Induced Anxiety and Reward Inhibition [RNA-Seq stress]

Project description:STAT3S727 Phosphorylation in VTA Dopaminergic Neurons Competed by O-GlcNAcylation Regulates Acute Stress-Induced Anxiety and Reward Inhibition [RNA-Seq stress]

| PRJNA1155615 | ENA

TET2 and TET3 regulate GlcNAcylation and H3K4 methylation through OGT and SET1/COMPASS

Project description:TET proteins convert 5-methylcytosine to 5-hydroxymethylcytosine, an emerging dynamic epigenetic state of DNA that can influence transcription. Evidence has linked TET1 function to epigenetic repression complexes, yet mechanistic information, especially for the TET2 and TET3 proteins, remains limited. Here, we show a direct interaction of TET2 and TET3 with O-GlcNAc transferase (OGT). OGT does not appear to influence hmC activity, rather TET2 and TET3 promote OGT activity. TET2/3-OGT co-localize on chromatin at active promoters enriched for H3K4me3 and reduction of either TET2/3 or OGT activity results in a direct decrease in H3K4me3 and concomitant decreased transcription. Further, we show that Host Cell Factor 1 (HCF1), a component of the H3K4 methyltransferase SET1/COMPASS complex, is a specific GlcNAcylation target of TET2/3-OGT, and modification of HCF1 is important for the integrity of SET1/COMPASS. Additionally, we find both TET proteins and OGT activity promote binding of the SET1/COMPASS H3K4 methyltransferase, SETD1A, to chromatin. Finally, studies in Tet2 knockout mouse bone marrow tissue extend and support the data as decreases are observed of global GlcNAcylation and also of H3K4me3, notably at several key regulators of haematopoiesis. Together, our results unveil a step-wise model, involving TET-OGT interactions, promotion of GlcNAcylation, and influence on H3K4me3 via SET1/COMPASS, highlighting a novel means by which TETs may induce transcriptional activation. ChIP-Seq experiments were performed on Illumina HiScanSQ sequencer in wild-type HEK293T cells for H3K4me3 histone marks, O-GlcNAc and HCF1, for HT-TET2, HT-TET3 and HT-OGT in HEK293T cells overexpressing those three fusion proteins and in TET2 Kd HEK293T cells for H3K4me3 histone marks. ChIP-Seqs were also performed in mouse bone marrow tissues for H3K4me3 histone marks, O-GlcNAc, endogenous Tet2 and in Tet2 Ko bone marrow tissues for H3K4me3 histone marks.

2013-02-07 | E-GEOD-36620 | biostudies-arrayexpress

Dot1L recruits OGT target chromatin to regulate histones O-GlcNAcylation

Project description:OGT (O-GlcNAc transferase) is the distinctive enzyme responsible for catalyzing O-GlcNAc to the serine or threonine residues of thousands of cytoplasm and nuclear proteins that are involved in DNA damage, RNA splicing, and transcription preinitiation and initiation complex assembly. However, the molecular mechanism by OGT regulating gene transcription remains elusive. Using proximity labeling based mass spectrometry, we searched for functional partners of OGT and found that Dot1L, the conserved and unique histone methyltransferase mediated histone H3 lys79 methylation required for gene transcription, DNA damage repair, cell proliferation, and embryo development, interacts with OGT. Although this specific interaction does not regulate the enzymatic activity of Dot1L, it facilitates OGT-dependent histones O-GlcNAcylation. Moreover, OGT associates with Dot1L at transcription start sites, and depleting Dot1L decreased OGT associated with chromatin globally. Notably, downregulation of Dot1L reduces the levels of histone H2B S112 O-GlcNAcylation and histone H2B K120 ubiquitination in vivo, which are associated with gene transcription regulation. Taken together, these results reveal a Dot1L-dependent O-GlcNAcylation of chromatin.

2022-04-06 | GSE200059 | GEO

TET2 and TET3 regulate GlcNAcylation and H3K4 methylation through OGT and SET1/COMPASS

2013-02-07 | GSE36620 | GEO

FBXO31-mediated Ubiquitination of OGT Maintains O-GlcNAcylation Homeostasis to Restrain Endometrial Malignancy

Project description:CRISPR screen and biochemical characterization reveal that tumor suppressor F-box only protein 31 (FBXO31) regulates O-GlcNAcylation homeostasis in EC by ubiquitinating the O-GlcNAc transferase OGT.

2025-01-23 | GSE287788 | GEO

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