Source:http://linkedlifedata.com/resource/pubmed/id/20374709
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rdf:type | |
lifeskim:mentions | |
pubmed:dateCreated |
2010-4-8
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pubmed:abstractText |
Transcriptional regulation by nuclear hormone receptors (NRs) requires multiple coregulators that modulate chromatin structures by catalyzing a diverse array of posttranslational modifications of histones. Different combinations of these modifications yield dynamic functional outcomes, constituting an epigenetic histone code. This code is inscribed by histone-modifying enzymes and decoded by effector proteins that recognize specific covalent marks. One important modification associated with active chromatin structures is methylation of histone H3-lysine 4 (H3K4). Crucial roles for this modification in NR transactivation have been recently highlighted through our purification and subsequent characterization of a steady-state complex associated with ASC-2, a coactivator of NRs and other transcription factors. This complex, designated ASCOM for ASC-2 complex, contains H3K4-methyltransferase MLL3/HALR or its paralogue MLL4/ALR and represents the first Set1-like H3K4-methyltransferase complex to be reported in vertebrates. This review focuses on recent progress in our understanding of how ASCOM-MLL3 and ASCOM-MLL4 influence NR-mediated gene transcription and of their physiological function.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Histone-Lysine N-Methyltransferase,
http://linkedlifedata.com/resource/pubmed/chemical/Histones,
http://linkedlifedata.com/resource/pubmed/chemical/Lysine,
http://linkedlifedata.com/resource/pubmed/chemical/Multiprotein Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cytoplasmic and Nuclear,
http://linkedlifedata.com/resource/pubmed/chemical/histone methyltransferase
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pubmed:status |
MEDLINE
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pubmed:issn |
1878-0814
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pubmed:author | |
pubmed:copyrightInfo |
Copyright © 2009 Elsevier Inc. All rights reserved.
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pubmed:issnType |
Electronic
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pubmed:volume |
87
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
343-82
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pubmed:meshHeading |
pubmed-meshheading:20374709-Animals,
pubmed-meshheading:20374709-Histone-Lysine N-Methyltransferase,
pubmed-meshheading:20374709-Histones,
pubmed-meshheading:20374709-Humans,
pubmed-meshheading:20374709-Lysine,
pubmed-meshheading:20374709-Multiprotein Complexes,
pubmed-meshheading:20374709-Receptors, Cytoplasmic and Nuclear,
pubmed-meshheading:20374709-Transcription, Genetic
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pubmed:year |
2009
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pubmed:articleTitle |
Roles of histone H3-lysine 4 methyltransferase complexes in NR-mediated gene transcription.
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pubmed:affiliation |
Department of Molecular and Human Genetics, Baylor College of Medicine, Houston, Texas 77030, USA.
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pubmed:publicationType |
Journal Article,
Review,
Research Support, N.I.H., Extramural
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