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http://hdl.handle.net/10261/24372
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Campo DC | Valor | Lengua/Idioma |
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dc.contributor.author | Jiménez Lara, Ana M. | - |
dc.contributor.author | Aranda, Ana | - |
dc.date.accessioned | 2010-05-17T11:19:38Z | - |
dc.date.available | 2010-05-17T11:19:38Z | - |
dc.date.issued | 1999-06 | - |
dc.identifier.citation | Faseb Journal 13(9): 1073-1081 (1999) | en_US |
dc.identifier.issn | 0892-6638 | - |
dc.identifier.uri | http://hdl.handle.net/10261/24372 | - |
dc.description | 9 pages, 6 figures. | en_US |
dc.description.abstract | Heterodimers of the vitamin D receptor (VDR) with the retinoid X receptor (RXR) bind in a transcriptionally unproductive manner to the retinoic acid response element present in the retinoic acid receptor-ß2 promoter. This element is composed of a direct repeat (DR) of the sequence PuGTTCA spaced by five nucleotides. However, the same sequence separated by three nucleotides (DR3) acts as a strong vitamin D response element. Here we show that the polarity of binding of the heterodimers to the DR3 was 5'-RXR-VDR-3', whereas on the DR5, both heterodimeric partners bind indistinctly to the 5' or 3' hemi-sites. These results suggest that the response elements can allosterically regulate the conformation of the receptors to determine positive or negative regulation of gene expression. Despite the altered polarity, the DR5-bound heterodimer was able to recruit the nuclear receptor coactivator ACTR in a vitamin D-dependent fashion. Furthermore, binding of the corepressor SMRT (silencing mediator of retinoid and thyroid hormone receptors) to the RXR/VDR heterodimer on a DR5 was not observed. Binding of RXR/VDR heterodimers to DRs with different transcriptional outcomes may generate selectivity and provide a greater complexity and flexibility to the vitamin D responses.—Jimenez-Lara, A. M., Aranda, A. The vitamin D receptor binds in a transcriptionally inactive form and without a defined polarity on a retinoic acid response element. | en_US |
dc.description.sponsorship | This work has been supported by grants PB94–0094 from the DGICYT and PM97–0135 from the DGES. | en_US |
dc.format.extent | 395946 bytes | - |
dc.format.mimetype | application/pdf | - |
dc.language.iso | eng | en_US |
dc.publisher | Federation of American Societies for Experimental Biology | en_US |
dc.rights | closedAccess | en_US |
dc.subject | Retinoid receptor | en_US |
dc.subject | Half-site | en_US |
dc.subject | Heterodimer | en_US |
dc.subject | Retinoid X receptor | en_US |
dc.title | The vitamin D receptor binds in a transcriptionally inactive form and without a defined polarity on a retinoic acid response element | en_US |
dc.type | artículo | en_US |
dc.description.peerreviewed | Peer reviewed | en_US |
dc.relation.publisherversion | http://www.fasebj.org/cgi/pmidlookup?view=long&pmid=10336890 | en_US |
dc.type.coar | http://purl.org/coar/resource_type/c_6501 | es_ES |
item.languageiso639-1 | en | - |
item.fulltext | No Fulltext | - |
item.openairecristype | http://purl.org/coar/resource_type/c_18cf | - |
item.cerifentitytype | Publications | - |
item.grantfulltext | none | - |
item.openairetype | artículo | - |
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