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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
2004-3-2
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pubmed:abstractText |
The cellular function of the menin tumor suppressor protein, product of the MEN1 gene mutated in familial multiple endocrine neoplasia type 1, has not been defined. We now show that menin is associated with a histone methyltransferase complex containing two trithorax family proteins, MLL2 and Ash2L, and other homologs of the yeast Set1 assembly. This menin-associated complex methylates histone H3 on lysine 4. A subset of tumor-derived menin mutants lacks the associated histone methyltransferase activity. In addition, menin is associated with RNA polymerase II whose large subunit carboxyl-terminal domain is phosphorylated on Ser 5. Men1 knockout embryos and cells show decreased expression of the homeobox genes Hoxc6 and Hoxc8. Chromatin immunoprecipitation experiments reveal that menin is bound to the Hoxc8 locus. These results suggest that menin activates the transcription of differentiation-regulating genes by covalent histone modification, and that this activity is related to tumor suppression by MEN1.
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pubmed:grant |
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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/Chromatin,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Histone-Lysine N-Methyltransferase,
http://linkedlifedata.com/resource/pubmed/chemical/MEN1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Methyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Methyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Trl protein, Drosophila,
http://linkedlifedata.com/resource/pubmed/chemical/histone methyltransferase
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
1097-2765
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pubmed:author |
pubmed-author:BhattacharjeeArindamA,
pubmed-author:BiondiChristine ACA,
pubmed-author:CopelandTerry DTD,
pubmed-author:HayesD NeilDN,
pubmed-author:HaywardNicholas KNK,
pubmed-author:HessJay LJL,
pubmed-author:HughesChristina MCM,
pubmed-author:KayGraham FGF,
pubmed-author:LeeJeffrey CJC,
pubmed-author:LevineStuart SSS,
pubmed-author:MeyersonMatthewM,
pubmed-author:MilneThomas ATA,
pubmed-author:Rozenblatt-RosenOritO,
pubmed-author:ShanmugamKalai SelviKS
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pubmed:issnType |
Print
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pubmed:day |
27
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pubmed:volume |
13
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
587-97
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:14992727-Animals,
pubmed-meshheading:14992727-Cells, Cultured,
pubmed-meshheading:14992727-Chromatin,
pubmed-meshheading:14992727-DNA-Binding Proteins,
pubmed-meshheading:14992727-Drosophila Proteins,
pubmed-meshheading:14992727-Fibroblasts,
pubmed-meshheading:14992727-Gene Expression Regulation, Neoplastic,
pubmed-meshheading:14992727-Genes, Homeobox,
pubmed-meshheading:14992727-Genes, Tumor Suppressor,
pubmed-meshheading:14992727-HeLa Cells,
pubmed-meshheading:14992727-Histone-Lysine N-Methyltransferase,
pubmed-meshheading:14992727-Humans,
pubmed-meshheading:14992727-Methyltransferases,
pubmed-meshheading:14992727-Mice,
pubmed-meshheading:14992727-Mice, Knockout,
pubmed-meshheading:14992727-Protein Methyltransferases,
pubmed-meshheading:14992727-Proto-Oncogene Proteins,
pubmed-meshheading:14992727-Transcription Factors
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pubmed:year |
2004
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pubmed:articleTitle |
Menin associates with a trithorax family histone methyltransferase complex and with the hoxc8 locus.
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pubmed:affiliation |
Department of Medical Oncology, Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA 02115, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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