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ATF4 regulates MYB to increase g-globin in response to loss of β-globin

ABSTRACT: This SuperSeries is composed of the SubSeries listed below.

ORGANISM(S): Homo sapiens

PROVIDER: GSE153768 | GEO | 2020/07/26

REPOSITORIES: GEO

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ATF4 regulates MYB to increase g-globin in response to loss of β-globin [ChIP-seq]

Project description:Boontanrart et al model the cellular stress that occurs upon reduction in β-globin in human erythroid cells. Decrease in β-globin attenuates the eIF2aP-ATF4 pathway and results in upregulating fetal -globin. Down-regulation of ATF4 leads to decreased levels of the -globin repressor MYB through direct binding at the HBS1L-MYB intergenic region.

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ATF4 regulates MYB to increase g-globin in response to loss of β-globin [RNA-seq]

Project description:Boontanrart et al model the cellular stress that occurs upon reduction in β-globin in human erythroid cells. Decrease in β-globin attenuates the eIF2aP-ATF4 pathway and results in upregulating fetal g-globin. Down-regulation of ATF4 leads to decreased levels of the g-globin repressor MYB through direct binding at the HBS1L-MYB intergenic region.

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ATF4 regulates MYB to increase g-globin in response to loss of β-globin

Project description:ATF4 regulates MYB to increase g-globin in response to loss of β-globin

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ATF4 regulates MYB to increase g-globin in response to loss of β-globin [ChIP-seq]

Project description:ATF4 regulates MYB to increase g-globin in response to loss of β-globin [ChIP-seq]

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ATF4 regulates MYB to increase g-globin in response to loss of β-globin [RNA-seq]

Project description:ATF4 regulates MYB to increase g-globin in response to loss of β-globin [RNA-seq]

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Chromosomal loop engineering in human beta globin locus

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PRMT5 regulates ATF4 transcript splicing and oxidative stress response.

Project description:Protein methyltransferase 5 (PRMT5) symmetrically dimethylates arginine residues leading to regulation of transcription and splicing programs. Although PRMT5 has emerged as an attractive oncology target, the molecular determinants of PRMT5 dependency in cancer remain incompletely understood. Our transcriptomic analysis identified PRMT5 regulation of the activating transcription factor 4 (ATF4) pathway in acute myelogenous leukemia (AML). PRMT5 inhibition resulted in the expression of unstable, intron-retaining ATF4 mRNA that is detained in the nucleus. Concurrently, the decrease in the spliced cytoplasmic transcript of ATF4 led to lower levels of ATF4 protein and downregulation of ATF4 target genes. Upon loss of functional PRMT5, cells with low ATF4 displayed increased oxidative stress, growth arrest, and cellular senescence. Interestingly, leukemia cells with EVI1 oncogene overexpression demonstrated dependence on PRMT5 function. EVI1 and ATF4 regulated gene signatures were inversely correlated. We show that EVI1-high AML cells have reduced ATF4 levels, elevated baseline reactive oxygen species and increased sensitivity to PRMT5 inhibition. Thus, EVI1-high cells demonstrate dependence on PRMT5 function and regulation of oxidative stress response. Overall, our findings identify the PRMT5-ATF4 axis to be safeguarding the cellular redox balance that is especially important in high oxidative stress states, such as those that occur with EVI1 overexpression.

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