| pubmed-article:17317671 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17317671 | lifeskim:mentions | umls-concept:C1235660 | lld:lifeskim |
| pubmed-article:17317671 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:17317671 | lifeskim:mentions | umls-concept:C0079419 | lld:lifeskim |
| pubmed-article:17317671 | lifeskim:mentions | umls-concept:C1422120 | lld:lifeskim |
| pubmed-article:17317671 | lifeskim:mentions | umls-concept:C1704735 | lld:lifeskim |
| pubmed-article:17317671 | pubmed:issue | 16 | lld:pubmed |
| pubmed-article:17317671 | pubmed:dateCreated | 2007-4-16 | lld:pubmed |
| pubmed-article:17317671 | pubmed:abstractText | Members of the evolutionarily conserved Mastermind (MAM) protein family, including the three related mammalian Mastermind-like (MAML) proteins MAML1-3, function as crucial coactivators of Notch-mediated transcriptional activation. Given the recent evidence of cross-talk between the p53 and Notch signal transduction pathways, we have investigated whether MAML1 may also be a transcriptional coactivator of p53. Indeed, we show here that MAML1 is able to interact with p53. We show that MAML1-p53 interaction involves the N-terminal region of MAML1 and the DNA-binding domain of p53, and we use a chromatin immunoprecipitation assay to show that MAML1 is part of the activator complex that binds to native p53-response elements within the promoter of the p53 target genes. Overexpression of wild-type MAML1 as well as a mutant, defective in Notch signaling, enhanced the p53-dependent gene induction in mammalian cells, whereas MAML1 knockdown reduced the p53-dependent gene expression. MAML1 increases the half-life of p53 protein and enhances its phosphorylation/acetylation upon DNA damage of cells. Finally, RNA interference-mediated knockdown of the single Caenorhabditis elegans MAML homolog, Lag-3, led to substantial abrogation of p53-mediated germ-cell apoptotic response to DNA damage and markedly reduced the expression of Ced-13 and Egl-1, downstream pro-apoptotic targets of the C. elegans p53 homolog Cep-1. Thus, we present evidence for a novel coactivator function of MAML1 for p53, independent of its function as a coactivator of Notch signaling pathway. | lld:pubmed |
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| pubmed-article:17317671 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:17317671 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:17317671 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17317671 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:17317671 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:17317671 | pubmed:author | pubmed-author:GriffinJames... | lld:pubmed |
| pubmed-article:17317671 | pubmed:author | pubmed-author:ZhangYingY | lld:pubmed |
| pubmed-article:17317671 | pubmed:author | pubmed-author:MieleLucioL | lld:pubmed |
| pubmed-article:17317671 | pubmed:author | pubmed-author:MATSIu NIuN | lld:pubmed |
| pubmed-article:17317671 | pubmed:author | pubmed-author:BandHamidH | lld:pubmed |
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| pubmed-article:17317671 | pubmed:author | pubmed-author:BandVimlaV | lld:pubmed |
| pubmed-article:17317671 | pubmed:author | pubmed-author:ReddiHoney... | lld:pubmed |
| pubmed-article:17317671 | pubmed:author | pubmed-author:ZhaoYongtongY | lld:pubmed |
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| pubmed-article:17317671 | pubmed:author | pubmed-author:WuLiziL | lld:pubmed |
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| pubmed-article:17317671 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17317671 | pubmed:day | 20 | lld:pubmed |
| pubmed-article:17317671 | pubmed:volume | 282 | lld:pubmed |
| pubmed-article:17317671 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17317671 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17317671 | pubmed:pagination | 11969-81 | lld:pubmed |
| pubmed-article:17317671 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:17317671 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17317671 | pubmed:articleTitle | The notch regulator MAML1 interacts with p53 and functions as a coactivator. | lld:pubmed |
| pubmed-article:17317671 | pubmed:affiliation | Division of Cancer Biology, Department of Medicine, ENH Research Institute, Feinberg School of Medicine, Northwestern University, Evanston, Illinois 60201, USA. | lld:pubmed |
| pubmed-article:17317671 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17317671 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:17317671 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:17317671 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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