PLU-1 Is an H3K4 demethylase involved in transcriptional repression and breast cancer cell proliferation Journal Article

  

Authors:	Yamane, K.; Tateishi, K.; Klose, R. J.; Fang, J.; Fabrizio, L. A.; Erdjument-Bromage, H.; Taylor-Papadimitriou, J.; Tempst, P.; Zhang, Y.
Article Title:	PLU-1 Is an H3K4 demethylase involved in transcriptional repression and breast cancer cell proliferation
Abstract:	Posttranslational modification of chromatin by histone methylation has wide-ranging effects on nuclear function, including transcriptional regulation, maintenance of genome integrity, and epigenetic inheritance. The enzymes utilized to place histone methylation marks are well characterized, but the identity of a histone demethylation system remained elusive until recently. The discovery of histone demethylase enzymes capable of directly removing methyl groups from modified lysine residues has demonstrated that histone methylation is a dynamic modification. The most extensive family of histone demethylase enzymes identified so far contains a JmjC domain and catalyzes demethylation through a hydroxylation reaction. Here, we identify PLU-1, a transcriptional repressor implicated in breast cancer, as a histone demethylase enzyme that has the ability to reverse the trimethyl H3K4 modification state. Furthermore, we reveal that PLU-1-mediated H3K4 demethylase activity plays an important role in the proliferative capacity of breast cancer cells through repression of tumor suppressor genes, including BRCA1. © 2007 Elsevier Inc. All rights reserved.
Keywords:	unclassified drug; dna-binding proteins; nonhuman; protein domain; protein function; cell proliferation; cell cycle; cell division; breast cancer; transcription, genetic; enzyme activity; cell line, tumor; breast neoplasms; nuclear proteins; tumor suppressor gene; gene expression regulation, neoplastic; dna; protein processing; transcription regulation; amino acid sequence; molecular sequence data; enzyme analysis; histone h3; gene repression; repressor proteins; breast carcinogenesis; genetic epigenesis; protein methylation; histone deacetylase; protein modification; regulator protein; hydroxylation; histone demethylase; protein plu 1
Journal Title:	Molecular Cell
Volume:	25
Issue:	6
ISSN:	1097-2765
Publisher:	Cell Press
Date Published:	2007-03-23
Start Page:	801
End Page:	812
Language:	English
DOI:	10.1016/j.molcel.2007.03.001
PUBMED:	17363312
PROVIDER:	scopus
DOI/URL:	http://www.scopus.com/inward/record.url?eid=2-s2.0-33947244845&partnerID=40&md5=775381a4077fb371f963deab4d235d5e
Notes:	--- - "Cited By (since 1996): 108" - "Export Date: 17 November 2011" - "CODEN: MOCEF" - "Source: Scopus"

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