pubmed-article:19596783 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:19596783 | lifeskim:mentions | umls-concept:C0079427 | lld:lifeskim |
pubmed-article:19596783 | lifeskim:mentions | umls-concept:C0025267 | lld:lifeskim |
pubmed-article:19596783 | lifeskim:mentions | umls-concept:C1325410 | lld:lifeskim |
pubmed-article:19596783 | lifeskim:mentions | umls-concept:C1418776 | lld:lifeskim |
pubmed-article:19596783 | lifeskim:mentions | umls-concept:C1159884 | lld:lifeskim |
pubmed-article:19596783 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
pubmed-article:19596783 | pubmed:issue | 18 | lld:pubmed |
pubmed-article:19596783 | pubmed:dateCreated | 2009-8-27 | lld:pubmed |
pubmed-article:19596783 | pubmed:abstractText | Menin, the product of the MEN1 (multiple endocrine neoplasia type 1) tumor suppressor gene, is involved in activation of gene transcription as part of an MLL1 (mixed-lineage leukemia 1)/MLL2 (KMT2A/B)-containing protein complex which harbors methyltransferase activity for lysine 4 of histone H3 (H3K4). As MEN1 patients frequently develop lipomas and peroxisome proliferator-activated receptor gamma (PPARgamma) is expressed in several MEN1-related tumor types, we investigated regulation of PPARgamma activity by menin. We found that menin is required for adipocyte differentiation of murine 3T3-L1 cells and PPARgamma-expressing mouse embryonic fibroblasts. Menin augments PPARgamma target gene expression through recruitment of H3K4 methyltransferase activity. Menin interacts directly with the activation function 2 transcription activation domain of PPARgamma in a ligand-independent fashion. Ligand-dependent coactivation, however, is dependent on the LXXLL motif of menin and the intact helix 12 of PPARgamma. We propose that menin is an important factor in PPARgamma-mediated adipogenesis and that loss of PPARgamma function may contribute to lipoma development in MEN1 patients. | lld:pubmed |
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pubmed-article:19596783 | pubmed:language | eng | lld:pubmed |
pubmed-article:19596783 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19596783 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:19596783 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:19596783 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:19596783 | pubmed:month | Sep | lld:pubmed |
pubmed-article:19596783 | pubmed:issn | 1098-5549 | lld:pubmed |
pubmed-article:19596783 | pubmed:author | pubmed-author:KummerJ... | lld:pubmed |
pubmed-article:19596783 | pubmed:author | pubmed-author:LipsCornelis... | lld:pubmed |
pubmed-article:19596783 | pubmed:author | pubmed-author:KalkhovenEric... | lld:pubmed |
pubmed-article:19596783 | pubmed:author | pubmed-author:JeningaEllen... | lld:pubmed |
pubmed-article:19596783 | pubmed:author | pubmed-author:HöppenerJo... | lld:pubmed |
pubmed-article:19596783 | pubmed:author | pubmed-author:TimmersH T... | lld:pubmed |
pubmed-article:19596783 | pubmed:author | pubmed-author:VarierRadhika... | lld:pubmed |
pubmed-article:19596783 | pubmed:author | pubmed-author:DreijerinkKoe... | lld:pubmed |
pubmed-article:19596783 | pubmed:author | pubmed-author:van... | lld:pubmed |
pubmed-article:19596783 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:19596783 | pubmed:volume | 29 | lld:pubmed |
pubmed-article:19596783 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:19596783 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:19596783 | pubmed:pagination | 5060-9 | lld:pubmed |
pubmed-article:19596783 | pubmed:dateRevised | 2010-9-24 | lld:pubmed |
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