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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
2005-2-9
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pubmed:abstractText |
Changes in the substrate specificities of factors that irreversibly modify the histone components of chromatin are expected to have a profound effect on gene expression through epigenetics. Ezh2 is a histone-lysine methyltransferase with activity dependent on its association with other components of the Polycomb Repressive Complexes 2 and 3 (PRC2/3). Ezh2 levels are increasingly elevated during prostate cancer progression. Other PRC2/3 components also are elevated in cancer cells. Overexpression of Ezh2 in tissue culture promotes formation of a previously undescribed PRC complex, PRC4, that contains the NAD+-dependent histone deacetylase SirT1 and isoform 2 of the PRC component Eed. Eed2 is expressed in cancer and undifferentiated embryonic stem (ES) cells but is undetectable in normal and differentiated ES cells. The distinct PRCs exhibit differential histone substrate specificities. These findings suggest that formation of a transformation-specific PRC complex may have a major role in resetting patterns of gene expression by regulating chromatin structure.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/15684044-11498575,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15684044-11571273,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15684044-11850410,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15684044-11854455,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15684044-12036903,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15684044-12067650,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15684044-12086602,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15684044-12351676,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15684044-12374981,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15684044-12408863,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15684044-12408864,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15684044-12435631,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15684044-12533679,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15684044-12689588,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15684044-12873978,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15684044-14500907,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15684044-14532106,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15684044-14585615,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15684044-14666671,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15684044-15020040,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15684044-15099518,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15684044-15225548,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15684044-15231737,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15684044-15469825,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15684044-15498488,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15684044-9214638,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15684044-9742080
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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/EZH2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Eed protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Ezh2 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Histone-Lysine N-Methyltransferase,
http://linkedlifedata.com/resource/pubmed/chemical/Histones,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Isoforms,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Sirt1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Sirtuin 1,
http://linkedlifedata.com/resource/pubmed/chemical/Sirtuins,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/polycomb group proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0027-8424
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pubmed:author |
pubmed-author:Abate-ShenCoryC,
pubmed-author:BrockdorffNeilN,
pubmed-author:FarnhamPeggyP,
pubmed-author:KirmizisAntonisA,
pubmed-author:KuzmichevAndreiA,
pubmed-author:MargueronRaphaelR,
pubmed-author:OuyangXuesongX,
pubmed-author:PreissnerTanja STS,
pubmed-author:ReinbergDannyD,
pubmed-author:ScherMichaelM,
pubmed-author:VaqueroAlejandroA
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pubmed:issnType |
Print
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pubmed:day |
8
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pubmed:volume |
102
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1859-64
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:15684044-Humans,
pubmed-meshheading:15684044-Animals,
pubmed-meshheading:15684044-Mice,
pubmed-meshheading:15684044-Proteins,
pubmed-meshheading:15684044-Prostatic Neoplasms,
pubmed-meshheading:15684044-Histones,
pubmed-meshheading:15684044-Male,
pubmed-meshheading:15684044-Cell Differentiation,
pubmed-meshheading:15684044-Macromolecular Substances,
pubmed-meshheading:15684044-HeLa Cells,
pubmed-meshheading:15684044-Substrate Specificity,
pubmed-meshheading:15684044-Repressor Proteins,
pubmed-meshheading:15684044-Protein Isoforms,
pubmed-meshheading:15684044-Gene Expression Regulation,
pubmed-meshheading:15684044-Multigene Family,
pubmed-meshheading:15684044-DNA-Binding Proteins,
pubmed-meshheading:15684044-Transcription Factors,
pubmed-meshheading:15684044-Histone-Lysine N-Methyltransferase,
pubmed-meshheading:15684044-Gene Expression Profiling
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