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Etoposide promotes tumor cells pyroptosis via down-regulation of O-GlcNAcylation to regulating p53 stability

ABSTRACT: Etoposide promotes tumor cells pyroptosis via down-regulation of O-GlcNAcylation to regulating p53 stability

PROVIDER: PRJNA1105635 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR28824527_1.fastq.gz	Fastqsanger.gz
	SRR28824527_2.fastq.gz	Fastqsanger.gz
	SRR28824528_1.fastq.gz	Fastqsanger.gz
	SRR28824528_2.fastq.gz	Fastqsanger.gz
	SRR28824529_1.fastq.gz	Fastqsanger.gz

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Etoposide promotes tumor cells pyroptosis via down-regulation of O-GlcNAcylation to regulating p53 stability

Project description:As a new type of cell death mediated by Gasdermin (GSDM) family, pyroptosis has increasingly become a research hotspot in the fields of biology and medicine. Studies have found that a variety of drugs (such as etoposide and traditional Chinese medicine extracts) can effectively inhibit the occurrence and development of tumors by activating caspase family and GSDM protein family to induce pyroptosis. Promoting pyroptosis has become an effective method for the treatment of tumors, but the research on its regulatory mechanism is still lacking. In order to explore the key molecular pathways of etoposide-induced pyroptosis, transcriptome sequencing analysis was performed

2024-11-20 | GSE266073 | GEO

Dynamic O-GlcNAcylation coordinates etoposide-triggered tumor cell pyroptosis by regulating p53 stability.

Project description:O-GlcNAcylation, a modification of nucleocytoplasmic proteins in mammals, plays a critical role in various cellular processes. However, the interplay and their underlying mechanisms in chemotherapy-induced tumor regression between O-GlcNAcylation and pyroptosis, a form of programmed cell death associated with innate immunity, remains unclear. Here, we observed that during the etoposide-induced pyroptosis of SH-SY5Y and A549 cells, overall O-GlcNAcylation levels are substantially reduced. Pharmacological inhibition or genetic manipulation of O-GlcNAcylation, such as OGT inhibition or OGA overexpression, sensitized these cells to etoposide-induced pyroptosis both in vitro and in vivo. Mechanistically, mutations at S96 and S149 residues attenuated p53 O-GlcNAcylation, weakening its interaction with MDM2, reducing p53 ubiquitination, and increasing protein stability. These results suggest that S96 may be a putative O-GlcNAcylation site. Therefore, p53 target genes-Fas, DR-5, Puma, and PIDD-were transcriptionally upregulated, leading to activation of the caspase-3-GSDME axis and promoting etoposide-induced pyroptosis in various tumor cells. This study demonstrates a previously uncharacterized association between O-GlcNAcylation and chemotherapy-induced pyroptosis, offering potential therapeutic interventions for pyroptosis-related diseases.

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Mutant p53 cooperates with ETS2 to promote etoposide resistance

Project description:This SuperSeries is composed of the following subset Series: GSE36749: Mutant p53 cooperates with ETS2 to promote etoposide resistance [ChIP-Seq] GSE36751: Mutant p53 cooperates with ETS2 to promote etoposide resistance [ChIP-chip] Refer to individual Series

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GlcNAcylation of histone H2B facilitates its monoubiquitination

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p53 binding and chromatin dynamics after etoposide treatment of primary lung fibroblast

Project description:We report the chromatin modification dynamics at p53 binding sites afte 6 hours of treatment of etoposide (100 micromolar final) in IMR90 human lung fibroblasts using ChIP-seq , ATAC-seq, and polyA+ RNA-seq analyses. We assessed the genomewide occupancy of histone H3, H3K4me3, H3K4me2, H3K4me1, H3K27ac, H4K16ac, RNA polymerase II, p53, and transposase-accessible chromatin (ATAC-seq) in response to etoposide treatment.

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

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Mutant p53 cooperates with ETS2 to promote etoposide resistance [ChIP-chip]

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Project description:The transcription factor FOXA1, which functions in epigenetic reprogramming, plays a critical role in breast cancer progression. However, the molecular mechanisms by which FOXA1 achieves its oncogenic functions remain elusive. Here, we demonstrate that the O-GlcNAcylation of FOXA1 increases breast cancer metastasis capacity by orchestrating the transcription of numerous metastasis regulators. O-GlcNAcylation at Thr432, Ser441 and Ser443 regulates the stability of FOXA1 and promotes its assembly with chromatin in breast cancer cells. We provide evidence that O-GlcNAcylation shapes the FOXA1 interactome, especially triggering the recruitment of the transcriptional repressor MECP2 and consequently stimulating FOXA1 chromatin-binding sites to switch to chromatin loci of adhesion-related genes, including EPB41L3 and COL9A2. Site-specific depletion of O-GlcNAcylation on FOXA1 affects the expression of various downstream genes and thus inhibits breast cancer proliferation and metastasis both in vitro and in vivo.

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FOXA1 O-GlcNAcylation-mediated transcriptional switch governs metastasis capacity in breast cancer [ChIP-seq]

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