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Lactate regulates major zygotic genome activation by H3K18 lactylation in mammals [RNA-seq]

ABSTRACT: Lactate regulates major zygotic genome activation by H3K18 lactylation in mammals [RNA-seq]

PROVIDER: PRJNA979207 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR24821167_1.fastq.gz	Fastqsanger.gz
	SRR24821167_2.fastq.gz	Fastqsanger.gz
	SRR24821168_1.fastq.gz	Fastqsanger.gz
	SRR24821168_2.fastq.gz	Fastqsanger.gz
	SRR24821169_1.fastq.gz	Fastqsanger.gz

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Lactate regulates major zygotic genome activation by H3K18 lactylation in mammals

Project description:Lactate regulates major zygotic genome activation by H3K18 lactylation in mammals

| PRJNA979204 | ENA

Lactate regulates major zygotic genome activation by H3K18 lactylation in mammals [CUT&TAG]

Project description:Lactate regulates major zygotic genome activation by H3K18 lactylation in mammals [CUT&TAG]

| PRJNA979206 | ENA

Lactate regulates major zygotic genome activation by H3K18 lactylation in mammals [CUT&TAG]

Project description:Lactate is present at a high level in the microenvironment of mammalian preimplantation embryos in vivo and in vitro. However, its role in preimplantation development is unclear. Here, we report that lactate is highly enriched in the nuclei of early embryos when major zygotic genome activation (ZGA) occurs in humans and mice. The inhibition of its production and uptake results in developmental arrest at the 2-cell stage, major ZGA failure, and loss of lactate-derived H3K18lac, and the abnormal phenotypes could be recapitulated by overexpression of H3K18R mutation and rescued by addition of Lac-CoA. By profiling the landscape of H3K18lac in human and mouse preimplantation embryos, we show that H3K18lac is enriched on the promoter regions of most major ZGA genes and corelates with their expressions. Taken together, we demonstrate the important role for lactate in major ZGA via H3K18lac, showing a conserved metabolic mechanism underlies preimplantation development of mammalian embryos.

2024-02-14 | GSE234026 | GEO

Lactate regulates major zygotic genome activation by H3K18 lactylation in mammals [RNA-seq]

2024-02-14 | GSE234025 | GEO

Lactate regulates major zygotic genome activation by H3K18 lactylation in mammals

Project description: Not available

| S-EPMC10849771 | biostudies-literature

BRD9 Reads Lactate-Induced H3K18 Lactylation to Drive Oncogenic Chromatin Remodeling in Hepatocellular Carcinoma

Project description:Histone lactylation bridges glycolytic metabolism to oncogenic transcription, but its mechanistic readers remain poorly defined. Here, we identify bromodomain-containing protein 9 (BRD9) as a lactyl-lysine reader that links lactate-driven H3K18 lactylation (H3K18la) to chromatin remodeling in hepatocellular carcinoma (HCC). Clinically, elevated H3K18la levels correlate with poor HCC prognosis. Structural (NMR) and biophysical analyses demonstrate BRD9’s bromodomain engages H3K18la through its acetyl-lysine pocket with weak, transient affinity, distinct from stable H3K18ac binding, enabling lactate-dependent chromatin interactions. Multi-omics profiling reveals H3K18la recruits BRD9 and the non-canonical BRG1-associated factor (ncBAF) complex to active enhancers and promoters, promoting chromatin accessibility and oncogenic transcription (SPARC, TMEM64, ANGEL1, SCARB1). Glycolytic inhibition or BRD9 targeting displaces BRD9 from chromatin, suppresses oncogenes, and impairs HCC proliferation. p300 or HDAC inhibition attenuates H3K18la-driven oncogenic transcription and tumor viability. Our findings establish BRD9 as a metabolic-epigenetic mediator that translates glycolytic flux into chromatin remodeling, offering actionable therapeutic targets for HCC.

2026-03-05 | GSE314155 | GEO

Lactate-Induced H3K18 Lactylation Drives CX3CL1-Mediated Immune Cell Recruitment in Sepsis-Associated ARDS

Project description:Sepsis is characterized by lactate accumulation and immune dysfunction, but the molecular mechanisms linking lactate to chemokine expression remain unclear. Here, we investigated whether lactate regulates chemokine transcription through histone lactylation. Human peripheral blood mononuclear cells (PBMCs) were treated with lactate (LAC group) or PBS control (CON group), followed by RNA sequencing (RNA-seq) to identify differentially expressed genes. Chromatin immunoprecipitation sequencing (ChIP-seq) using H3K18la-specific antibody was performed to detect lactylation-enriched gene promoters. Integration of RNA-seq and ChIP-seq data identified CX3CL1 as a lactylation-regulated chemokine. Functional assays demonstrated that lactate-induced H3K18la promotes CX3CL1 expression, enhances PBMC migration, and facilitates T cell recruitment in vitro. In a cecal ligation and puncture (CLP)-induced sepsis-associated acute respiratory distress syndrome (ARDS) mouse model, elevated lactate increased pulmonary CX3CL1 expression and immune cell infiltration, whereas inhibition of lactate production reduced these effects. These data reveal a lactate–H3K18la–CX3CL1 axis that mediates immune cell recruitment and exacerbates sepsis-related lung injury.

2026-04-22 | GSE328660 | GEO

Lactate promotes cholesterol uptake by facilitating SCARB1 expression through histone H3K18 lactylation

Project description:Lactate promotes cholesterol uptake by facilitating SCARB1 expression through histone H3K18 lactylation

| PRJNA1330274 | ENA

Mesenchymal stem cell–derived extracellular vesicles alleviate immunoparalysis in sepsis-associated ARDS via reprogramming the lactate–H3K18 lactylation–PSMD14 axis

Project description:Sepsis-associated acute respiratory distress syndrome (S-ARDS) is characterized by immune dysfunction and high mortality. Here, we show that elevated lactate induces P300-dependent H3K18 lactylation, which enhances PSMD14 transcription. Increased PSMD14 activates the AKT/mTOR pathway, leading to macrophage immunosuppression, including reduced inflammatory cytokine production, impaired phagocytosis, increased M2 polarization, and T cell dysfunction.Integrated analyses of public datasets, RNA-seq, and ChIP-seq identified PSMD14 as a key immune-related gene associated with poor outcomes and reduced HLA-DR expression in patients. Extracellular vesicles derived from P300 inhibitor (C646)-preconditioned mesenchymal stem cells suppress the H3K18la–PSMD14 axis, restore immune function, and improve survival.

2026-04-07 | GSE327100 | GEO

Lactate-driven H3K18 lactylation promotes cisplatin resistance in bladder cancer via HNRNPF-Parkin mediated mitophagy

Project description:Cisplatin resistance in bladder cancer (BCa) is driven by metabolic reprogramming that enhances glycolysis and lactate production. Here, we report that lactate-induced histone H3K18 lactylation (H3K18la) drives chemoresistance by activating a novel signaling axis that couples epigenetic regulation with mitochondrial quality control. Through integrative multi-omics analysis, we identified HNRNPF as a key effector downstream of H3K18la, with its promoter being directly enriched by H3K18la in cisplatin-resistant BCa cells. Unexpectedly, HNRNPF, primarily known as an RNA-binding protein, promotes chemoresistance through a non-canonical mechanism: it directly interacts with the core mitophagy protein Parkin. Mechanistically, the RRM2 domain of HNRNPF binds the R0 domain of Parkin, facilitating Parkin’s recruitment to damaged mitochondria. This interaction potentiates Parkin’s E3 ubiquitin ligase activity, leading to enhanced ubiquitination of VDAC1 and robust activation of mitophagy. Collectively, our findings establish the H3K18la-HNRNPF-Parkin axis as a previously unrecognized signaling cascade that bridges epigenetic reprogramming with to mitochondrial quality control in chemoresistance. Targeting this axis, particularly the HNRNPF-Parkin interaction or mitophagy activation, may represent a novel therapeutic strategy to overcome cisplatin resistance in BCa, pending further validation in preclinical models.

2026-03-30 | GSE325983 | GEO

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