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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
14
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pubmed:dateCreated |
2007-7-19
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pubmed:abstractText |
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 DUSP1 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 DUSP1 and that DUSP1 is a link between E2F-1 and MAP kinases.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0008-5472
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
67
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
6737-44
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:17638884-Amino Acid Motifs,
pubmed-meshheading:17638884-Apoptosis,
pubmed-meshheading:17638884-Base Sequence,
pubmed-meshheading:17638884-Cell Cycle Proteins,
pubmed-meshheading:17638884-Cell Line, Tumor,
pubmed-meshheading:17638884-Dual Specificity Phosphatase 1,
pubmed-meshheading:17638884-E2F1 Transcription Factor,
pubmed-meshheading:17638884-Gene Expression Regulation, Neoplastic,
pubmed-meshheading:17638884-Humans,
pubmed-meshheading:17638884-Immediate-Early Proteins,
pubmed-meshheading:17638884-MAP Kinase Signaling System,
pubmed-meshheading:17638884-Molecular Sequence Data,
pubmed-meshheading:17638884-Neurons,
pubmed-meshheading:17638884-Oxidative Stress,
pubmed-meshheading:17638884-Phosphoprotein Phosphatases,
pubmed-meshheading:17638884-Promoter Regions, Genetic,
pubmed-meshheading:17638884-Protein Phosphatase 1,
pubmed-meshheading:17638884-Protein Tyrosine Phosphatases,
pubmed-meshheading:17638884-Transcription, Genetic,
pubmed-meshheading:17638884-Transfection
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pubmed:year |
2007
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pubmed:articleTitle |
Dual specificity phosphatase 1/CL100 is a direct transcriptional target of E2F-1 in the apoptotic response to oxidative stress.
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pubmed:affiliation |
Department of Radiation Oncology, Center for Radiological Research, College of Physicians and Surgeons, Columbia University Medical Center, 630 West 168th Street, New York, NY 10032, USA.
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pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural
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