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Hexokinase 2 and lactate mediated gene expression via histone H3 lysine 18 lactylation (CHO CUT&Tag)

ABSTRACT: Hexokinase 2 and lactate mediated gene expression via histone H3 lysine 18 lactylation (CHO CUT&Tag)

PROVIDER: PRJNA953055 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR24099873_1.fastq.gz	Fastqsanger.gz
	SRR24099873_2.fastq.gz	Fastqsanger.gz
	SRR24099874_1.fastq.gz	Fastqsanger.gz
	SRR24099874_2.fastq.gz	Fastqsanger.gz
	SRR24099875_1.fastq.gz	Fastqsanger.gz

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Hexokinase 2 and lactate mediated gene expression via histone H3 lysine 18 lactylation (CHO RNA-Seq)

Project description:Hexokinase catalyzes the first committed step in glucose metabolism by phosphorylating glucose to produce glucose-6-phosphate. Highly glycolytic proliferating cells such as cancer cells take advantage of HK2 expression to accelerate glucose metabolism even in the presence of oxygen. This acceleration not only provides sufficient glycolytic intermediates to support the anabolic demands of the cells but also inevitably accompanies increased formation of metabolic end products such as lactate. Currently, the effect of lactate caused by HK2-mediated metabolic alteration is largely unknown. A recent study found that lactate plays a role in an epigenetic alteration known as histone lactylation. Here, using RNA-seq and CUT&Tag chromatin profiling, we study the effect of HK2 and lactate on gene expression via histone lactylation (H3K18la).

2023-05-05 | GSE229153 | GEO

Hexokinase 2 and lactate mediated gene expression via histone H3 lysine 18 lactylation (CHO CUT&Tag)

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Hexokinase 2 and lactate mediated gene expression via histone H3 lysine 18 lactylation (CHO RNA-Seq)

Project description:Hexokinase 2 and lactate mediated gene expression via histone H3 lysine 18 lactylation (CHO RNA-Seq)

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Hexokinase 2-mediated gene expression via histone lactylation is required for hepatic stellate cell activation and liver fibrosis (CUT&Tag)

Project description:Lactate was implicated in activation of hepatic stellate cells (HSCs). However, the mechanism by which lactate exerts its effect remains elusive. We show that hexokinase 2 (HK2) is sufficient to change gene expression by histone lactylation but not histone acetylation. Using RNA-seq and CUT&Tag chromatin profiling, we found that induction of HK2 expression in activated HSCs is required for the induced gene expression by elevating histone lactylation. Inhibiting histone lactylation by Hk2 deletion or pharmacological inhibition of lactate production diminishes HSC activation, whereas exogenous lactate but not acetate supplementation rescues the activation phenotype. Thus, lactate produced by activated HSCs determines the HSC fate via histone lactylation. We found that histone acetylation competes with histone lactylation, which could explain why class I HDAC inhibitors impede HSC activation. Finally, HSC-specific or systemic deletion of HK2 inhibits HSC activation and liver fibrosis in vivo. Therefore, we provide evidence that HK2 may be an effective therapeutic target for liver fibrosis.

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2024-11-23 | PXD057709 | Pride

Global Lysine Lactylation Dynamics during HCMV and HSV-1 Infections

Project description:Aerobic glycolysis is a hallmark of virus-infected cells, leading to substantial accumulation and secretion of lactate. However, the regulatory roles of lactate during viral infections are still poorly understood. Here, we report that human cytomegalovirus (HCMV) infection leverages lactate to induce widespread protein lactylation and promote viral spread. Lactyllysine decorates intrinsically disordered regions (IDRs) of proteins, regulating viral protein condensates and immune signaling transduction. Dynamic lactylation of immune response pathways, a feature shared during infection with herpes simplex virus 1 (HSV-1), suppresses immunity through regulation of HEXIM1, RBM14, and IFI16. K90 lactylation of the viral DNA sensor IFI16 blocks recruitment of the DNA-damage response master kinase DNA-PK, preventing IFI16-driven gene repression and cytokine responses. Together, we characterize global protein lactylation dynamics during virus infection, finding virus-induced lactate contributes to its immune evasion through direct inhibition of immune signaling pathways.

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