| pubmed-article:11073980 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11073980 | lifeskim:mentions | umls-concept:C0812201 | lld:lifeskim |
| pubmed-article:11073980 | lifeskim:mentions | umls-concept:C0015127 | lld:lifeskim |
| pubmed-article:11073980 | lifeskim:mentions | umls-concept:C0206588 | lld:lifeskim |
| pubmed-article:11073980 | lifeskim:mentions | umls-concept:C1314792 | lld:lifeskim |
| pubmed-article:11073980 | lifeskim:mentions | umls-concept:C0004083 | lld:lifeskim |
| pubmed-article:11073980 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:11073980 | pubmed:issue | 23 | lld:pubmed |
| pubmed-article:11073980 | pubmed:dateCreated | 2000-12-19 | lld:pubmed |
| pubmed-article:11073980 | pubmed:abstractText | The vitamin D receptor (VDR) normally functions as a ligand-dependent transcriptional activator. Here we show that, in the presence of Ets-1, VDR stimulates the prolactin promoter in a ligand-independent manner, behaving as a constitutive activator. Mutations in the AF2 domain abolish vitamin D-dependent transactivation but do not affect constitutive activation by Ets-1. Therefore, in contrast with the actions of vitamin D, activation by Ets-1 is independent of the AF2 domain. Ets-1 also conferred a ligand-independent activation to the estrogen receptor and to peroxisome proliferator-activated receptor alpha. In addition, Ets-1 cooperated with the unliganded receptors to stimulate the activity of reporter constructs containing consensus response elements fused to the thymidine kinase promoter. There is a direct interaction of the receptors with Ets-1 which requires the DNA binding domains of both proteins. Interaction with Ets-1 induces a conformational change in VDR which can be detected by an increased resistance to proteolytic digestion. Furthermore, a retinoid X receptor-VDR heterodimer in which both receptors lack the core C-terminal AF2 domain can recruit coactivators in the presence, but not in the absence, of Ets-1. This suggests that Ets-1 induces a conformational change in the receptor which creates an active interaction surface with coactivators even in the AF2-defective mutants. These results demonstrate the existence of a novel mechanism, alternative to ligand binding, which can convert an unliganded receptor from an inactive state into a competent transcriptional activator. | lld:pubmed |
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| pubmed-article:11073980 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11073980 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11073980 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:11073980 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11073980 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:11073980 | pubmed:issn | 0270-7306 | lld:pubmed |
| pubmed-article:11073980 | pubmed:author | pubmed-author:ArandaAA | lld:pubmed |
| pubmed-article:11073980 | pubmed:author | pubmed-author:TolónR MRM | lld:pubmed |
| pubmed-article:11073980 | pubmed:author | pubmed-author:CastilloA IAI | lld:pubmed |
| pubmed-article:11073980 | pubmed:author | pubmed-author:Jiménez-LaraA... | lld:pubmed |
| pubmed-article:11073980 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11073980 | pubmed:volume | 20 | lld:pubmed |
| pubmed-article:11073980 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11073980 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11073980 | pubmed:pagination | 8793-802 | lld:pubmed |
| pubmed-article:11073980 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:11073980 | pubmed:year | 2000 | lld:pubmed |
