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SET1B facilitates activation of the hypoxia response through site-specific histone methylation

ABSTRACT: SET1B facilitates activation of the hypoxia response through site-specific histone methylation

PROVIDER: PRJNA715190 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR13989881_1.fastq.gz	Fastqsanger.gz
	SRR13989881_2.fastq.gz	Fastqsanger.gz
	SRR13989882_1.fastq.gz	Fastqsanger.gz
	SRR13989882_2.fastq.gz	Fastqsanger.gz
	SRR13989883_1.fastq.gz	Fastqsanger.gz

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SET1B facilitates activation of the hypoxia response through site-specific histone methylation

Project description:Hypoxia-inducible transcription factors (HIFs) are fundamental to the cellular adaptation to low oxygen levels but how they interact with chromatin and efficiently activate their target genes is unclear. Using genome-wide mutagenesis in human cancer cells, we define genes required for HIF transcriptional activation, and identify a requirement for the Histone 3 lysine 4 (H3K4) methyltransferase SET1B. Loss of SET1B leads to a selective reduction in HIF transcriptional activity in hypoxia, with SET1B driving expression of genes involved in angiogenesis rather than glycolysis, resulting in impaired tumour establishment in SET1B deficient xenografts. Mechanistically, we show that SET1B is itself oxygen regulated, accumulates on chromatin in hypoxia, and is recruited to HIF target genes through HIF-1a. Accordingly, we show that the hypoxic induction of H3K4me3 at specific HIF targets is both HIF and SET1B dependent, and when impaired, decreases promotor acetylation and gene expression. Together, these findings reveal SET1B as a determinant of site-specific histone methylation and provide insight into how HIF target genes are differentially regulated.

2021-05-04 | GSE169087 | GEO

SET1B facilitates activation of the hypoxia response through site-specific histone methylation [ChIP-seq_1]

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SET1B facilitates activation of the hypoxia response through site-specific histone methylation [ChIP-seq_2]

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SET1B facilitates activation of the hypoxia response through site-specific histone methylation

Project description:SET1B facilitates activation of the hypoxia response through site-specific histone methylation

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SET1B facilitates activation of the hypoxia response through site-specific histone methylation [ChIP-seq_1]

Project description:SET1B facilitates activation of the hypoxia response through site-specific histone methylation [ChIP-seq_1]

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SET1B facilitates activation of the hypoxia response through site-specific histone methylation [ChIP-seq_2]

Project description:SET1B facilitates activation of the hypoxia response through site-specific histone methylation [ChIP-seq_2]

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SET1B facilitates activation of the hypoxia response through site-specific histone methylation

Project description:This SuperSeries is composed of the SubSeries listed below.

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Hypoxia promotes histone H3K9 lactylation to enhance LAMC2 transcription in esophageal squamous cell carcinoma

Project description:Hypoxia promotes tumorigenesis and lactate accumulation in esophageal squamous cell carcinoma (ESCC). Lactate can induce histone lysine lactylation (Kla, a recently-identified histone marks) to regulate transcription. However, the functional consequence of histone Kla under hypoxia in ESCC remains to be explored. Here, we reveal that hypoxia facilitates histone H3K9la to enhance LAMC2 transcription for proliferation of ESCC. We found that global level of Kla was elevated under hypoxia, and thus identified the landscape of histone Kla in ESCC by quantitative proteomics. Furthermore, we show a significant increase of H3K9la level induced by hypoxia. Next, MNseq ChIP-seq and RNA-seq analysis suggest that H3K9la is enriched at the promoter of cell junction genes. Finally, we demonstrate that the histone H3K9la facilitates the expression of LAMC2 for ESCC invasion by in vivo and in vitro experiments. Briefly, our study reveal a vital role of histone Kla triggered by hypoxia in cancer.

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Project description:Epithelial Hypoxia-Inducible Factor 2α Facilitates the Progression of Colon Tumors through Recruiting Neutrophils

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