| pubmed-article:17475621 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17475621 | lifeskim:mentions | umls-concept:C0001128 | lld:lifeskim |
| pubmed-article:17475621 | lifeskim:mentions | umls-concept:C0085732 | lld:lifeskim |
| pubmed-article:17475621 | lifeskim:mentions | umls-concept:C2745900 | lld:lifeskim |
| pubmed-article:17475621 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
| pubmed-article:17475621 | lifeskim:mentions | umls-concept:C0004083 | lld:lifeskim |
| pubmed-article:17475621 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:17475621 | lifeskim:mentions | umls-concept:C1880177 | lld:lifeskim |
| pubmed-article:17475621 | pubmed:issue | 25 | lld:pubmed |
| pubmed-article:17475621 | pubmed:dateCreated | 2007-6-18 | lld:pubmed |
| pubmed-article:17475621 | pubmed:abstractText | The aberrant association of promyelocytic leukemia protein-retinoic acid receptor-alpha (PML-RARalpha) with corepressor complexes is generally thought to contribute to the ability of PML-RARalpha to regulate transcription. We report here that PML-RARalpha acquires aberrant association with coactivators. We show that endogenous PML-RARalpha interacts with the histone acetyltransferases CBP, p300, and SRC-1 in a hormoneindependent manner, an association not seen for RARalpha. This hormone-independent coactivator binding activity requires an intact ligand-binding domain and the NR box of the coactivators. Confocal microscopy studies demonstrate that exogenous PML-RARalpha sequesters and colocalizes with coactivators. These observations correlate with the ability of PML-RARalpha to attenuate the transcription activation of the Notch signaling downstream effector, CBF1, and of the glucocorticoid receptor. This includes attenuation of the glucocorticoid-induced leucine zipper (GILZ) and FLJ25390 target genes of the endogenous glucocorticoid receptor. Furthermore, treatment of NB4 cells with all-trans-retinoic acid, which promotes PML-RARalpha degradation, resulted in increased activation of GILZ. On the basis of these findings, we propose a model in which the hormone-independent association between PML-RARalpha and coactivators contributes to its ability to regulate gene expression. | lld:pubmed |
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| pubmed-article:17475621 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:17475621 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:17475621 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17475621 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:17475621 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:17475621 | pubmed:author | pubmed-author:ItôMM | lld:pubmed |
| pubmed-article:17475621 | pubmed:author | pubmed-author:KaoHung-YingH... | lld:pubmed |
| pubmed-article:17475621 | pubmed:author | pubmed-author:LamMinhM | lld:pubmed |
| pubmed-article:17475621 | pubmed:author | pubmed-author:LiuHengH | lld:pubmed |
| pubmed-article:17475621 | pubmed:author | pubmed-author:ReinekeErin... | lld:pubmed |
| pubmed-article:17475621 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17475621 | pubmed:day | 22 | lld:pubmed |
| pubmed-article:17475621 | pubmed:volume | 282 | lld:pubmed |
| pubmed-article:17475621 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17475621 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17475621 | pubmed:pagination | 18584-96 | lld:pubmed |
| pubmed-article:17475621 | pubmed:dateRevised | 2007-12-3 | lld:pubmed |
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| pubmed-article:17475621 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17475621 | pubmed:articleTitle | Aberrant association of promyelocytic leukemia protein-retinoic acid receptor-alpha with coactivators contributes to its ability to regulate gene expression. | lld:pubmed |
| pubmed-article:17475621 | pubmed:affiliation | Department of Biochemistry, School of Medicine, Case Western Reserve University, and the Research Institute of University Hospitals of Cleveland, OH 44106, USA. | lld:pubmed |
| pubmed-article:17475621 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17475621 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:17475621 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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