Cloos PA, Christensen J, Agger K, Helin K.. Erasing the methyl mark: histone demethylases at the center of cellular differentiation and disease. Genes Dev 22: 1115-1140

Biotech Research and Innovation Centre, University of Copenhagen, DK-2200 Copenhagen, Denmark.
Genes & Development (Impact Factor: 10.8). 06/2008; 22(9):1115-40. DOI: 10.1101/gad.1652908
Source: PubMed


The enzymes catalyzing lysine and arginine methylation of histones are essential for maintaining transcriptional programs and determining cell fate and identity. Until recently, histone methylation was regarded irreversible. However, within the last few years, several families of histone demethylases erasing methyl marks associated with gene repression or activation have been identified, underscoring the plasticity and dynamic nature of histone methylation. Recent discoveries have revealed that histone demethylases take part in large multiprotein complexes synergizing with histone deacetylases, histone methyltransferases, and nuclear receptors to control developmental and transcriptional programs. Here we review the emerging biochemical and biological functions of the histone demethylases and discuss their potential involvement in human diseases, including cancer.

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Available from: Karl Agger, May 12, 2014
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    • "On the other hand, histone methylation is a prerequisite for DNA methylation (Fuks, 2005; Fuks et al., 2003; Kondo, 2009; Lehnertz et al., 2003; Vire et al., 2006). Multiple histone acetyltransferases (Lee and Workman, 2007; Roth et al., 2001), deacetylases (Clayton et al., 2006; Mehnert and Kelly, 2007), methyltransferases (Greer and Shi, 2012; Teperino et al., 2010), and demethylases (Chen et al., 2012; Cloos et al., 2008; Lee et al., 2006; Wilson, 2007) have been discovered. Methylation of H3K9me3 and H3K27me3 leads to the formation of closed chromatin structure (heterochromatin) and thus marks transcriptional repression (Fuks, 2005; Kondo, 2009; Vire et al., 2006). "
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