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EZH2-mediated epigenetic suppression of IFNa/b-STAT2 signaling enhances anti-tumor immunity in breast cancer [RNA-Seq]

ABSTRACT: EZH2-mediated epigenetic suppression of IFNa/b-STAT2 signaling enhances anti-tumor immunity in breast cancer [RNA-Seq]

PROVIDER: PRJNA760910 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR15724336.fastq.gz	Fastqsanger.gz
	SRR15724337.fastq.gz	Fastqsanger.gz
	SRR15724338.fastq.gz	Fastqsanger.gz
	SRR15724339.fastq.gz	Fastqsanger.gz
	SRR15724340.fastq.gz	Fastqsanger.gz

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EZH2-mediated epigenetic suppression of IFNa/b-STAT2 signaling enhances anti-tumor immunity in breast cancer

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EZH2-mediated epigenetic suppression of IFNa/b-STAT2 signaling enhances anti-tumor immunity in breast cancer [ChIP-Seq]

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EZH2-mediated epigenetic suppression of IFNa/b-STAT2 signaling enhances anti-tumor immunity in breast cancer

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Expression data from primary human dermal fibroblasts with STAT2 deficiency and control fibroblasts treated with interferon

Project description:Primary human dermal fibroblasts were isolated from an individual showing a genetic defect in innate antiviral immunity associated with profound failure of type 1 interferon signaling and absence of the STAT2 protein. The transcriptional response of these cells to a 10h treatment with interferon-alpha was compared with that of control dermal fibroblasts. We used microarrays to detail the global program of gene expression resulting from interferon-alpha treatment in STAT 2 deficient and control fibroblasts. Primary human dermal fibroblasts were grown in the presence or absence of 1,000U/ml interferon-alpha (IFNa) for 10 hours before RNA extraction and hybridization on Affymetrix microarrays.

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Project description:STAT2 is an essential transcription factor in type I interferon (IFN) signaling. STAT2 is activated following exposure to IFN stimulation by phosphorylation at tyrosine-690. This post-translational modification permits the assembly and nuclear retention of the ISGF3 complex (consisting of STAT1/STAT2/IRF9) to drive gene transcription. We recently identified STAT2 to be serine phosphorylated in an IFN-dependent manner. The biological significance of these novel phosphorylation events in STAT2 remain to be elucidated. Thus far our data show that serine phosphorylation of STAT2 negatively regulates the biological effects of IFN. In an effort to understand the scope of STAT2 serine phosphorylation in IFN signaling, we conducted comparative microarray analysis to identify a collection of genes that are regulated by phosphorylated Ser734-STAT2 vs. unphosphorylated S734-STAT2 after IFN treatment.

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