| pubmed-article:19144644 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19144644 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:19144644 | lifeskim:mentions | umls-concept:C1334868 | lld:lifeskim |
| pubmed-article:19144644 | lifeskim:mentions | umls-concept:C0040845 | lld:lifeskim |
| pubmed-article:19144644 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:19144644 | lifeskim:mentions | umls-concept:C0032214 | lld:lifeskim |
| pubmed-article:19144644 | lifeskim:mentions | umls-concept:C0600138 | lld:lifeskim |
| pubmed-article:19144644 | lifeskim:mentions | umls-concept:C0597304 | lld:lifeskim |
| pubmed-article:19144644 | lifeskim:mentions | umls-concept:C1419025 | lld:lifeskim |
| pubmed-article:19144644 | lifeskim:mentions | umls-concept:C2587213 | lld:lifeskim |
| pubmed-article:19144644 | lifeskim:mentions | umls-concept:C1332838 | lld:lifeskim |
| pubmed-article:19144644 | pubmed:issue | 12 | lld:pubmed |
| pubmed-article:19144644 | pubmed:dateCreated | 2009-3-16 | lld:pubmed |
| pubmed-article:19144644 | pubmed:abstractText | Nuclear retinoic acid receptor alpha (RARalpha) activates gene expression through dynamic interactions with coregulatory protein complexes, the assembly of which is directed by the ligand and the AF-2 domain of RARalpha. Then RARalpha and its coactivator SRC-3 are degraded by the proteasome. Recently it has emerged that the proteasome also plays a key role in RARalpha-mediated transcription. Here we show that SUG-1, one of the six ATPases of the 19 S regulatory complex of the 26 S proteasome, interacts with SRC-3, is recruited at the promoters of retinoic acid (RA) target genes, and thereby participates to their transcription. In addition, SUG-1 also mediates the proteasomal degradation of SRC-3. However, when present in excess amounts, SUG-1 blocks the activation of RARalpha target genes and the degradation of RARalpha that occurs in response to RA, via its ability to interfere with the recruitment of SRC-3 and other coregulators at the AF-2 domain of RARalpha. We propose a model in which the ratio between SUG-1 and SRC-3 is crucial for the control of RARalpha functioning. This study provides new insights into how SUG-1 has a unique role in linking the transcription and degradation processes via its ability to interact with SRC-3. | lld:pubmed |
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| pubmed-article:19144644 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19144644 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19144644 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:19144644 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19144644 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:19144644 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:19144644 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19144644 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:19144644 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:19144644 | pubmed:author | pubmed-author:GarattiniEnri... | lld:pubmed |
| pubmed-article:19144644 | pubmed:author | pubmed-author:Rochette-Egly... | lld:pubmed |
| pubmed-article:19144644 | pubmed:author | pubmed-author:GianniMaurizi... | lld:pubmed |
| pubmed-article:19144644 | pubmed:author | pubmed-author:PlassatJean-L... | lld:pubmed |
| pubmed-article:19144644 | pubmed:author | pubmed-author:BruckNathalie... | lld:pubmed |
| pubmed-article:19144644 | pubmed:author | pubmed-author:LalevéeSébast... | lld:pubmed |
| pubmed-article:19144644 | pubmed:author | pubmed-author:RaskaIvanIJr | lld:pubmed |
| pubmed-article:19144644 | pubmed:author | pubmed-author:FerryChristin... | lld:pubmed |
| pubmed-article:19144644 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:19144644 | pubmed:day | 20 | lld:pubmed |
| pubmed-article:19144644 | pubmed:volume | 284 | lld:pubmed |
| pubmed-article:19144644 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19144644 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19144644 | pubmed:pagination | 8127-35 | lld:pubmed |
| pubmed-article:19144644 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
| pubmed-article:19144644 | pubmed:meshHeading | pubmed-meshheading:19144644... | lld:pubmed |
| pubmed-article:19144644 | pubmed:meshHeading | pubmed-meshheading:19144644... | lld:pubmed |
| pubmed-article:19144644 | pubmed:meshHeading | pubmed-meshheading:19144644... | lld:pubmed |
| pubmed-article:19144644 | pubmed:meshHeading | pubmed-meshheading:19144644... | lld:pubmed |
| pubmed-article:19144644 | pubmed:meshHeading | pubmed-meshheading:19144644... | lld:pubmed |
| pubmed-article:19144644 | pubmed:meshHeading | pubmed-meshheading:19144644... | lld:pubmed |
