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- W4361262513 abstract "<div>Abstract<p>E2F-1 mediates apoptosis through transcriptional regulation of its targets. We report here that E2F-1 acts as a direct transcriptional regulator of dual specificity phosphatase 1 (DUSP1; CL100), a threonine and tyrosine phosphatase that inhibits mitogen-activated protein (MAP) kinases. We found that DUSP1 is transcriptionally induced by ectopic E2F-1 expression and that extracellular signal–regulated kinase 1/2 are dephosphorylated in the presence of E2F-1 and DUSP1. E2F-1 mediates apoptosis in the cellular response to oxidative stress. DUSP1 levels are significantly increased in an E2F-1–dependent manner following oxidative stress but not other stresses examined. DUSP1 mediates the cellular response to oxidative stress. We found that E2F-1 binds to chromatin encompassing the DUSP1 promoter and greatly stimulates the promoter activity of the <i>DUSP1</i> gene. In particular, E2F-1 physically binds to an E2F-1 consensus sequence and a palindromic motif in the DUSP1 promoter. Interestingly, E2F-1 is acetylated following oxidative stress. Our findings show that E2F-1 is a transcriptional activator of <i>DUSP1</i> and that DUSP1 is a link between E2F-1 and MAP kinases. [Cancer Res 2007;67(14):6737–44]</p></div>" @default.
- W4361262513 created "2023-03-31" @default.
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- W4361262513 date "2023-03-30" @default.
- W4361262513 modified "2023-09-27" @default.
- W4361262513 title "Data from Dual Specificity Phosphatase 1/CL100 Is a Direct Transcriptional Target of E2F-1 in the Apoptotic Response to Oxidative Stress" @default.
- W4361262513 doi "https://doi.org/10.1158/0008-5472.c.6495908.v1" @default.
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