| pubmed-article:20615959 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:20615959 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:20615959 | lifeskim:mentions | umls-concept:C2348867 | lld:lifeskim |
| pubmed-article:20615959 | lifeskim:mentions | umls-concept:C2347946 | lld:lifeskim |
| pubmed-article:20615959 | pubmed:issue | 29 | lld:pubmed |
| pubmed-article:20615959 | pubmed:dateCreated | 2010-7-21 | lld:pubmed |
| pubmed-article:20615959 | pubmed:abstractText | Aire promotes the ectopic expression of a repertoire of peripheral-tissue antigens (PTAs) in thymic medullary epithelial cells (MECs) to mediate deletional tolerance and thereby prevent autoimmunity. Binding of hypomethylated histone 3 (H3)-tails by Aire's plant homeodomain (PHD) finger is essential for Aire function in cultured cell models, prompting speculation that Aire-PHD:H3-tail interactions underlie targeting of Aire to weakly transcribed loci. To evaluate the role of Aire's PHD finger in MECs on a global scale in vivo, we complemented Aire-deficient mice with a mutant of Aire that inhibits its binding to hypomethylated H3K4 residues. Although the range of Aire-targeted genes was largely unaffected in these mice, the D299A mutation caused a global dampening of Aire's transcriptional impact, resulting in an autoimmune disease similar in profile to that of their Aire-deficient counterparts. To test whether a low H3K4 methylation state is sufficient for Aire targeting, we overexpressed an H3K4-specific demethylase in an Aire-dependent cultured cell system, and determined its capacity to extend Aire's transcriptional footprint. The range and magnitude of Aire-regulated genes was largely unaffected, the only genes additionally induced by Aire in this context being those already accessed for repression. In short, Aire's H3-binding module is necessary for Aire-mediated regulation of gene expression and central tolerance induction, but this influence is unlikely to reflect a targeting mechanism solely based on the recognition of hypomethylated H3K4 residues. | lld:pubmed |
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| pubmed-article:20615959 | pubmed:language | eng | lld:pubmed |
| pubmed-article:20615959 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20615959 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:20615959 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:20615959 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:20615959 | pubmed:issn | 1091-6490 | lld:pubmed |
| pubmed-article:20615959 | pubmed:author | pubmed-author:KingstonRober... | lld:pubmed |
| pubmed-article:20615959 | pubmed:author | pubmed-author:BenoistChrist... | lld:pubmed |
| pubmed-article:20615959 | pubmed:author | pubmed-author:MathisDianeD | lld:pubmed |
| pubmed-article:20615959 | pubmed:author | pubmed-author:KohAndrew SAS | lld:pubmed |
| pubmed-article:20615959 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:20615959 | pubmed:day | 20 | lld:pubmed |
| pubmed-article:20615959 | pubmed:volume | 107 | lld:pubmed |
| pubmed-article:20615959 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:20615959 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:20615959 | pubmed:pagination | 13016-21 | lld:pubmed |
| pubmed-article:20615959 | pubmed:dateRevised | 2011-7-20 | lld:pubmed |
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| pubmed-article:20615959 | pubmed:year | 2010 | lld:pubmed |
| pubmed-article:20615959 | pubmed:articleTitle | Global relevance of Aire binding to hypomethylated lysine-4 of histone-3. | lld:pubmed |
| pubmed-article:20615959 | pubmed:affiliation | Department of Pathology, Harvard Medical School, Boston, MA 02115, USA. | lld:pubmed |
| pubmed-article:20615959 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:20615959 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:20615959 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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