pubmed-article:17000776 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:17000776 | lifeskim:mentions | umls-concept:C1332450 | lld:lifeskim |
pubmed-article:17000776 | lifeskim:mentions | umls-concept:C0162638 | lld:lifeskim |
pubmed-article:17000776 | lifeskim:mentions | umls-concept:C0019643 | lld:lifeskim |
pubmed-article:17000776 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
pubmed-article:17000776 | lifeskim:mentions | umls-concept:C0033414 | lld:lifeskim |
pubmed-article:17000776 | lifeskim:mentions | umls-concept:C1420556 | lld:lifeskim |
pubmed-article:17000776 | lifeskim:mentions | umls-concept:C1424530 | lld:lifeskim |
pubmed-article:17000776 | lifeskim:mentions | umls-concept:C1511737 | lld:lifeskim |
pubmed-article:17000776 | lifeskim:mentions | umls-concept:C1999177 | lld:lifeskim |
pubmed-article:17000776 | lifeskim:mentions | umls-concept:C1705630 | lld:lifeskim |
pubmed-article:17000776 | pubmed:issue | 23 | lld:pubmed |
pubmed-article:17000776 | pubmed:dateCreated | 2006-11-19 | lld:pubmed |
pubmed-article:17000776 | pubmed:abstractText | The antiapoptotic transcription factor NF-kappaB is constitutively activated in many cancers and is important for cytokine-mediated progression and metastatic movement of tumors. Breast cancer metastasis suppressor 1 (BRMS1) is a metastasis suppressor gene whose mechanisms of action are poorly understood. In this report, we demonstrate that BRMS1 decreases the transactivation potential of RelA/p65 and ameliorates the expression of NF-kappaB-regulated antiapoptotic gene products. BRMS1 immunoprecipitates with the RelA/p65 subunit of NF-kappaB with protein-protein interactions occurring at the C terminus region of the rel homology domain but not at its known transactivation domains. Moreover, BRMS1 functions as a corepressor by promoting binding of HDAC1 to RelA/p65, where it deacetylates lysine K310 on RelA/p65, which suppresses RelA/p65 transcriptional activity. Selective small interfering RNA knockdown of BRMS1 confirms that chromatin-bound BRMS1 is required for deacetylation of RelA/p65, while enhancing chromatin occupancy of HDAC1 onto the NF-kappaB-regulated promoters cIAP2 and Bfl-1/A1. We observed in cells lacking BRMS1 a dramatic increase in cell viability after the loss of attachment from the extracellular matrix. Collectively, these results suggest that BRMS1 suppresses metastasis through its ability to function as a transcriptional corepressor of antiapoptotic genes regulated by NF-kappaB. | lld:pubmed |
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pubmed-article:17000776 | pubmed:language | eng | lld:pubmed |
pubmed-article:17000776 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17000776 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:17000776 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:17000776 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17000776 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:17000776 | pubmed:month | Dec | lld:pubmed |
pubmed-article:17000776 | pubmed:issn | 0270-7306 | lld:pubmed |
pubmed-article:17000776 | pubmed:author | pubmed-author:LiuYuanY | lld:pubmed |
pubmed-article:17000776 | pubmed:author | pubmed-author:JonesDavid... | lld:pubmed |