| pubmed-article:15731352 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15731352 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:15731352 | lifeskim:mentions | umls-concept:C0003765 | lld:lifeskim |
| pubmed-article:15731352 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:15731352 | lifeskim:mentions | umls-concept:C0025723 | lld:lifeskim |
| pubmed-article:15731352 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:15731352 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:15731352 | lifeskim:mentions | umls-concept:C1879748 | lld:lifeskim |
| pubmed-article:15731352 | lifeskim:mentions | umls-concept:C1706853 | lld:lifeskim |
| pubmed-article:15731352 | pubmed:issue | 10 | lld:pubmed |
| pubmed-article:15731352 | pubmed:dateCreated | 2005-3-9 | lld:pubmed |
| pubmed-article:15731352 | pubmed:abstractText | Nuclear receptors activate transcription by recruiting multiple coactivators to the promoters of specific target genes. The functional synergy of the p160 coactivators [steroid receptor coactivator-1, glucocorticoid receptor interacting protein (GRIP1), or the activator for thyroid hormone and retinoid receptors], the histone acetyltransferases cAMP response element binding protein binding protein (CBP) and p300 and the histone methyltransferase coactivator-associated arginine methyltransferase (CARM1) depends on the methyltransferase activity of CARM1. CARM1 methylates histone H3 and other factors including the N-terminal region of p300. Here, we report that CARM1 also methylates Arg-2142 within the C-terminal GRIP1 binding domain (GBD) of p300. In the GBD, both Arg-2088 and Arg-2142 are important for binding GRIP1. Methylation of Arg-2142 inhibits the bimolecular interaction of GRIP1 to p300 in vitro and in vivo. This methylation mark of p300 GBD is removed by peptidyl deiminase 4, thereby enhancing the p300-GRIP1 interaction. These methylation and demethylimination events also alter the conformation and activity of the coactivator complex and regulate estrogen receptor-mediated transcription, and they thus represent unique mechanisms for regulating coactivator complex assembly, conformation, and function. | lld:pubmed |
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| pubmed-article:15731352 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:15731352 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:15731352 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15731352 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:15731352 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:15731352 | pubmed:author | pubmed-author:StallcupMicha... | lld:pubmed |
| pubmed-article:15731352 | pubmed:author | pubmed-author:CoonrodScott... | lld:pubmed |
| pubmed-article:15731352 | pubmed:author | pubmed-author:KrausW LeeWL | lld:pubmed |
| pubmed-article:15731352 | pubmed:author | pubmed-author:LeeYoung-HoYH | lld:pubmed |
| pubmed-article:15731352 | pubmed:author | pubmed-author:JelinekMary... | lld:pubmed |
| pubmed-article:15731352 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15731352 | pubmed:day | 8 | lld:pubmed |
| pubmed-article:15731352 | pubmed:volume | 102 | lld:pubmed |
| pubmed-article:15731352 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15731352 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15731352 | pubmed:pagination | 3611-6 | lld:pubmed |
| pubmed-article:15731352 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:15731352 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:15731352 | pubmed:articleTitle | Regulation of coactivator complex assembly and function by protein arginine methylation and demethylimination. | lld:pubmed |
| pubmed-article:15731352 | pubmed:affiliation | Department of Pathology, University of Southern California, 2011 Zonal Avenue, HMR 301, Los Angeles, CA 90089, USA. | lld:pubmed |
| pubmed-article:15731352 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15731352 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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