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Perturbation of O-GlcNAcylation homeostasis in Drosophila early embryos influences neurodevelopment by tuning facultative heterochromatin formation

ABSTRACT: Perturbation of O-GlcNAcylation homeostasis in Drosophila early embryos influences neurodevelopment by tuning facultative heterochromatin formation

PROVIDER: PRJNA809929 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR18121805_1.fastq.gz	Fastqsanger.gz
	SRR18121805_2.fastq.gz	Fastqsanger.gz
	SRR18121806_1.fastq.gz	Fastqsanger.gz
	SRR18121806_2.fastq.gz	Fastqsanger.gz
	SRR18121807_1.fastq.gz	Fastqsanger.gz

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Perturbation of O-GlcNAcylation homeostasis in Drosophila early embryos influences neurodevelopment by tuning facultative heterochromatin formation

Project description:Protein O-GlcNAcylation is a monosaccharide posttranslational modification maintained by two evolutionarily conserved enzymes, O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA). Mutations in human OGT have recently been associated with neurodevelopmental disorders, and yet whether and how the disturbed O-GlcNAcylation homeostasis impact the development of nervous system is not fully understood. Here, we generate transgenic Drosophila lines that conditionally express Clostridium perfringens OGA (CpOGA) to perturbate the homeostasis of protein O-GlcNAcylation. We reveal that lowering O-GlcNAcylation level, even just during early embryogenesis, can affect olfactory learning ability in adulthood. Mechanistically, decline of protein O-GlcNAcylation accompanies with emergence of facultative heterochromatin. The forced downregulation of global O-GlcNAcylation by exogenous CpOGA activity promotes nuclear foci formation of Polycomb-group protein Polyhomeotic (Ph) and accumulation of K27 trimethylation of histone H3 (H3K27me3), leading to enhanced facultative heterochromatin formation, which in turn interferes zygotic expression of several neurodevelopmental genes, particularly short of gastrulation (sog), a component of an evolutionarily conserved signaling system required for specification of neuroectoderm. Our findings highlight the importance of early embryonic O-GlcNAcylation homeostasis for the formation of a fully functional nervous system, casting new light on the etiology of OGT-associated intellectual disability.

2022-08-21 | GSE197343 | 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

GlcNAcylation of histone H2B facilitates its monoubiquitination [Illumina Genome Analyzer data]

Project description:We report that histone GlcNAcylation of H2B S112 is a vital histone modification which facilitates histone monoubiquitination (ub). In a genome-wide analysis, H2B S112 GlcNAcylation sites were observed widely distributed over entire chromosomes including transcribed gene loci, together with co-localization of H2B S112 GlcNAcylation and K120 ub. Examination of H2B S112 GlcNAc and H2B K120 ub in HeLa S3 cells

2011-10-27 | E-GEOD-33049 | biostudies-arrayexpress

5-hydroxymethylcytosine-mediated epigenetic dynamics during neurodevelopment and aging

Project description:This SuperSeries is composed of the following subset Series: GSE32050: 5-hydroxymethylcytosine-mediated epigenetic dynamics during neurodevelopment and aging [5hmC Capture and Seq] GSE32187: 5-hydroxymethylcytosine-mediated epigenetic dynamics during neurodevelopment and aging [mRNA profiling] Refer to individual Series

2011-10-29 | E-GEOD-32188 | biostudies-arrayexpress

GlcNAcylation of histone H2B facilitates its monoubiquitination [Illumina Genome Analyzer data]

2011-10-27 | GSE33049 | GEO

Ssdp influences neurodevelopment and autism-like behaviors in Drosophila melanogaster

Project description:Ssdp influences neurodevelopment and autism-like behaviors in Drosophila melanogaster

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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

Inhibition of O-GlcNAcylation via O-GlcNAc transferase fosters megakaryopoiesis and induces thrombopoiesis

Project description:We report that cellular O-GlcNAcylation levels decline along the course of megakaryocyte (MK) differentiation from human-derived hematopoietic stem and progenitor cells (HSPCs) and that inhibition of O-GlcNAc transferase (OGT), of which catalyzes O-GlcNAcylation, prolongedly decreases O-GlcNAcylation and induces megakaryopoiesis and thrombopoiesis. To gain the better insight into the potential mechanisms underlying platelet regulation by O-GlcNAcylation ,we compared the genome-wide transcription profiles of megakaryblastic MEG-01 cells with decreased O-GlcNAcylation (OGTi) and its control counterpart using RNA sequencing. Gene ontology and enrichment analysis of differentially expressed genes suggest that platelet formation might be regulated through the perturbation in cell adhesion molecules, i.e. integrin-a4 and b7, downstream of O-GlcNAc/c-Myc axis.

2020-08-06 | GSE150880 | GEO

O-GlcNAcylation of NONO is Critical for Paraspeckle Component Assembly and Contributes to Tumorigenesis

Project description:Non-POU domain-containing octamer-binding protein (NONO) is a multifunctional member of the Drosophila behavior/human splicing (DBHS) protein family with DNA- and RNA-binding activity. Recent studies revealed that NONO is O-GlcNAcylated and dysregulated in various types of cancer. Excessive O-GlcNAcylation of target proteins has also been implicated in tumorigenesis. However, it is not known whether O-GlcNAcylation of NONO promotes cancer cell growth, and little is known about the effect of O-GlcNAcylation on the biological properties of NONO. This study identifies Thr440 as the primary NONO O-GlcNAcylation site and demonstrates its crucial role in the assembly of paraspeckles, an important subnuclear compartment that facilitates NONO-dependent transcriptional regulation in mammalian cells. We demonstrated that O-GlcNAcylation of NONO is required to maintain the expression of genes related to GO category “microtubule cytoskeleton organization involved in mitosis” and to suppress the expression of genes related to GO category “cellular response to type I interferon”. Moreover, stable depletion of NONO O-GlcNAcylation or NONO knockout significantly inhibited the growth of colon cancer cells. These findings highlight the importance of NONO and its O-GlcNAcylation status in modulating cell cycle progression, immune response, and tumorigenesis.

2024-06-01 | GSE262460 | GEO

O-GlcNAcylation Mediates Wnt-stimulated Bone Formation via Rewiring Aerobic Glycolysis in Osteoblast-lineage Cells

Project description:As the efficient therapeutic treatment for osteoporosis, Wnt signaling is considered to induce bone formation through aerobic glycolysis. However, the mechanism underlying the regulatory role of Wnt in orchestrating glucose metabolism during osteogenesis remains unclear. O-GlcNAcylation, a dynamic posttranslational modification (PTM) on proteins, controls multiple critical biological processes including gene transcription, translation, and cell fate determination. Here, we report Wnt3a either induces O-GlcNAcylation rapidly via the Ca2+-PKA-Gfat1 axis, or increases it in a Wnt-β-catenin dependent manner during prolonged stimulation. Importantly, O-GlcNAcylation is found indispensable for osteoblastogenesis both in vivo and in vitro. Genetic ablation of O-GlcNAcylation in osteoblast-lineage cells diminishes bone formation and delays bone fracture healing in response to Wnt stimulation. Notably, Wnt3a-induced O-GlcNAcylation enhances aerobic glycolysis by stabilizing PDK1 partially through Serine 174 (S174) site, which consequently facilitates osteogenesis. These findings highlight that O-GlcNAcylation is indispensable in Wnt-induced glucose metabolism during osteogenesis, indicating its potential as a therapeutic target for osteoporosis.

2024-06-28 | GSE251951 | GEO

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