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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5849
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pubmed:dateCreated |
2007-10-19
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pubmed:abstractText |
Methylation of histone H3 lysine 27 (H3K27) is a posttranslational modification that is highly correlated with genomic silencing. Here we show that human UTX, a member of the Jumonji C family of proteins, is a di- and trimethyl H3K27 demethylase. UTX occupies the promoters of HOX gene clusters and regulates their transcriptional output by modulating the recruitment of polycomb repressive complex 1 and the monoubiquitination of histone H2A. Moreover, UTX associates with mixed-lineage leukemia (MLL) 2/3 complexes, and during retinoic acid signaling events, the recruitment of the UTX complex to HOX genes results in H3K27 demethylation and a concomitant methylation of H3K4. Our results suggest a concerted mechanism for transcriptional activation in which cycles of H3K4 methylation by MLL2/3 are linked with the demethylation of H3K27 through UTX.
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pubmed:grant |
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Histone Demethylases,
http://linkedlifedata.com/resource/pubmed/chemical/Histones,
http://linkedlifedata.com/resource/pubmed/chemical/Lysine,
http://linkedlifedata.com/resource/pubmed/chemical/MLL2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/MLL3 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Neoplasm Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Tretinoin,
http://linkedlifedata.com/resource/pubmed/chemical/UTX protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin,
http://linkedlifedata.com/resource/pubmed/chemical/polycomb group proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
1095-9203
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
19
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pubmed:volume |
318
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
447-50
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:17761849-Cell Differentiation,
pubmed-meshheading:17761849-Cell Line,
pubmed-meshheading:17761849-Cell Line, Tumor,
pubmed-meshheading:17761849-DNA-Binding Proteins,
pubmed-meshheading:17761849-Embryonic Stem Cells,
pubmed-meshheading:17761849-Genes, Homeobox,
pubmed-meshheading:17761849-Histone Demethylases,
pubmed-meshheading:17761849-Histones,
pubmed-meshheading:17761849-Humans,
pubmed-meshheading:17761849-Lysine,
pubmed-meshheading:17761849-Methylation,
pubmed-meshheading:17761849-Multigene Family,
pubmed-meshheading:17761849-Neoplasm Proteins,
pubmed-meshheading:17761849-Nuclear Proteins,
pubmed-meshheading:17761849-Promoter Regions, Genetic,
pubmed-meshheading:17761849-Protein Processing, Post-Translational,
pubmed-meshheading:17761849-Recombinant Proteins,
pubmed-meshheading:17761849-Repressor Proteins,
pubmed-meshheading:17761849-Signal Transduction,
pubmed-meshheading:17761849-Transcription, Genetic,
pubmed-meshheading:17761849-Transcriptional Activation,
pubmed-meshheading:17761849-Tretinoin,
pubmed-meshheading:17761849-Ubiquitin
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pubmed:year |
2007
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pubmed:articleTitle |
Demethylation of H3K27 regulates polycomb recruitment and H2A ubiquitination.
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pubmed:affiliation |
Wistar Institute, 3601 Spruce Street, Philadelphia, PA 19104, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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