| pubmed-article:20219974 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:20219974 | lifeskim:mentions | umls-concept:C0014939 | lld:lifeskim |
| pubmed-article:20219974 | lifeskim:mentions | umls-concept:C0031727 | lld:lifeskim |
| pubmed-article:20219974 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:20219974 | lifeskim:mentions | umls-concept:C1158537 | lld:lifeskim |
| pubmed-article:20219974 | pubmed:issue | 9 | lld:pubmed |
| pubmed-article:20219974 | pubmed:dateCreated | 2010-4-30 | lld:pubmed |
| pubmed-article:20219974 | pubmed:abstractText | Estrogens are suggested to play a role in the development and progression of proliferative diseases such as breast cancer. Like other steroid hormone receptors, the estrogen receptor-alpha (ERalpha) is a substrate of protein kinases, and phosphorylation has profound effects on its function and activity. Given the importance of DNA-dependent protein kinase (DNA-PK) for DNA repair, cell cycle progression, and survival, we hypothesized that it modulates ERalpha signaling. Here we show that, upon estrogen stimulation, DNA-PK forms a complex with ERalpha in a breast cancer cell line (MELN). DNA-PK phosphorylates ERalpha at Ser-118. Phosphorylation resulted in stabilization of ERalpha protein as inhibition of DNA-PK resulted in its proteasomal degradation. Activation of DNA-PK by double-strand breaks or its inhibition by siRNA technology demonstrated that estrogen-induced ERalpha activation and cell cycle progression is, at least, partially dependent on DNA-PK. | lld:pubmed |
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| pubmed-article:20219974 | pubmed:language | eng | lld:pubmed |
| pubmed-article:20219974 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20219974 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:20219974 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:20219974 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:20219974 | pubmed:month | May | lld:pubmed |
| pubmed-article:20219974 | pubmed:issn | 1939-4586 | lld:pubmed |
| pubmed-article:20219974 | pubmed:author | pubmed-author:SchmeisserAle... | lld:pubmed |
| pubmed-article:20219974 | pubmed:author | pubmed-author:Braun-Dullaeu... | lld:pubmed |
| pubmed-article:20219974 | pubmed:author | pubmed-author:MayerDorisD | lld:pubmed |
| pubmed-article:20219974 | pubmed:author | pubmed-author:MedunjaninSen... | lld:pubmed |
| pubmed-article:20219974 | pubmed:author | pubmed-author:WeinertSönkeS | lld:pubmed |
| pubmed-article:20219974 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:20219974 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:20219974 | pubmed:volume | 21 | lld:pubmed |
| pubmed-article:20219974 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:20219974 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:20219974 | pubmed:pagination | 1620-8 | lld:pubmed |
| pubmed-article:20219974 | pubmed:dateRevised | 2010-9-30 | lld:pubmed |
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