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Histone lactylation antagonizes senescence and skeletal muscle aging via facilitating gene expression reprogramming [CUT&Tag]

ABSTRACT: Histone lactylation antagonizes senescence and skeletal muscle aging via facilitating gene expression reprogramming [CUT&Tag]

PROVIDER: PRJNA938243 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR30930501_1.fastq.gz	Fastqsanger.gz
	SRR30930501_2.fastq.gz	Fastqsanger.gz
	SRR30930502_1.fastq.gz	Fastqsanger.gz
	SRR30930502_2.fastq.gz	Fastqsanger.gz
	SRR30930503_1.fastq.gz	Fastqsanger.gz

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Histone lactylation antagonizes senescence and skeletal muscle aging via facilitating gene expression reprogramming [CUT&Tag]

Project description:Epigenetic alterations are among the prominent drivers of cellular senescence and/or aging, intricately orchestrating gene expression programs during these processes. Many studies have investigated the histone modification mechanisms that regulate cellular senescence and aging. In this study, we show that histone lactylation, an identified histone modification that integrates metabolic processes, epigenetic regulation of gene expression and cellular activities in response to internal and external cues, plays a pivotal role in counteracting senescence and mitigating dysfunctions of skeletal muscle in aged mice. Mechanistically, histone lactylation levels markedly decrease during cellular senescence but are restored under hypoxic conditions primarily due to elevated glycolytic activity. The enrichment of histone lactylation at promoters is essential for sustaining the expression of genes involved in the cell cycle and DNA repair pathways, thereby inhibiting cellular senescence. Furthermore, the modulation of enzymes crucial for histone lactylation, including p300 and HDAC1, leads to reduced histone lactylation and accelerated cellular senescence. Consistently, the suppression of glycolysis and the depletion of histone lactylation are also observed during skeletal muscle aging. Running exercise increases the levels of glycolysis and histone lactylation, which in turn upregulate key genes in the DNA repair and proteostasis pathways, thereby helping to preserve the proper function of skeletal muscle. Our study highlights the significant roles of histone lactylation in modulating cellular senescence as well as aging-related tissue function, suggesting that this modification may serve as an innovative biomarker for senescence and provides a promising avenue for antiaging intervention via metabolic manipulation.

2024-05-01 | GSE226006 | GEO

Histone lactylation antagonizes senescence and skeletal muscle aging via facilitating gene expression reprogramming

Project description:Histone lactylation antagonizes senescence and skeletal muscle aging via facilitating gene expression reprogramming

| PRJNA938234 | ENA

Histone lactylation antagonizes senescence and skeletal muscle aging via facilitating gene expression reprogramming [snRNA-seq]

2024-05-01 | GSE226007 | GEO

Histone lactylation antagonizes senescence and skeletal muscle aging via facilitating gene expression reprogramming [RNA-seq]

2024-05-01 | GSE226005 | GEO

Histone lactylation antagonizes senescence and skeletal muscle aging via facilitating gene expression reprogramming [RNA-Seq II]

2024-05-01 | GSE249561 | GEO

Histone lactylation antagonizes senescence and skeletal muscle aging via facilitating gene expression reprogramming [RNA-seq]

Project description:Histone lactylation antagonizes senescence and skeletal muscle aging via facilitating gene expression reprogramming [RNA-seq]

| PRJNA938241 | ENA

Histone lactylation antagonizes senescence and skeletal muscle aging via facilitating gene expression reprogramming [snRNA-seq]

Project description:Histone lactylation antagonizes senescence and skeletal muscle aging via facilitating gene expression reprogramming [snRNA-seq]

| PRJNA938242 | ENA

Histone lactylation antagonizes senescence and skeletal muscle aging via facilitating gene expression reprogramming [RNA-Seq II]

Project description:Histone lactylation antagonizes senescence and skeletal muscle aging via facilitating gene expression reprogramming [RNA-Seq II]

| PRJNA1049487 | ENA

Genome-wide maps of histone lactylation in ocular melanoma by CUT&Tag

Project description:To investigate the function of histone lactylation in ocular melanoma, we analyzed histone lactylation enrichment level in ocular melanoma by CUT&Tag.

2023-09-04 | GSE242018 | GEO

DPF2 reads histone lactylation to drive transcription and tumorigenesis [CUT&TAG]

Project description:Lysine lactylation (Kla) is a new type of histone mark implicated in the regulation of various functional processes such as transcription. However, how this histone mark acts in cancers remains unexplored due in part to a lack of knowledge about its reader proteins. Here, we observe that cervical cancer (CC) cells undergo metabolic reprogram by which lactate accumulation and thereby boost histone lactylation, particularly H3K14la. Utilizing a multivalent photoaffinity probe in combination with quantitative proteomics approach, we identify DPF2 as a candidate target of H3K14la. Biochemical studies as well as CUT&Tag analysis reveal that DPF2 is capable of binding to H3K14la, and co-localizes with it on promoters of oncogenic genes. Notably, disrupting the association between DPF2 and histone lactylation through structure-guided mutation blunts those cancer-related gene expression along with cell survival. Together, our findings reveal DPF2 as a bona fide H3K14la effector that couples histone lactylation to gene transcription and cell survival, offering insight into how histone Kla engages in transcription and tumorigenesis.

2024-06-17 | GSE267109 | GEO

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