Chromatin Regulation / Acetylation

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The methylation state of lysine residues in histone proteins is a major determinant of the formation of active and inactive regions of the genome and is crucial for proper programming of the genome during development (1,2). Jumonji C (JmjC) domain-containing proteins represent the largest class of potential histone demethylase proteins (3). The JmjC domain can catalyze the demethylation of mono-, di-, and tri-methyl lysine residues via an oxidative reaction that requires iron and α-ketoglutarate (3). Based on homology, both humans and mice contain at least 30 such proteins, which can be divided into 7 separate families (3). The JMJD2 (Jumonji domain-containing protein 2) family, also known as JHDM3 (JmjC domain-containing histone demethylation protein 3) family, contains four members: JMJD2A/JHDM3A, JMJD2B/JHDM3B, JMJD2C/JHDM3C and JMJD2D/JHDM3D. In addition to the JmJC domain, these proteins also contain JmJN, PHD and Tudor domains, the latter of which has been shown to bind to methylated histone H3 at Lys4 and Lys9, and methylated histone H4 at Lys20 (4,5). JMJD2 proteins have been shown to demethylate di- and tri-methyl histone H3 at Lys9 and Lys36, and function as both activators and repressors of transcription (6-11). JMJD2A, JMJD2C and JMJD2D function as coactivators of the androgen receptor in prostate tumor cells (7). In contrast, JMJD2A also associates with Rb and N-CoR corepressor complexes and is necessary for transcriptional repression of target genes (8,9). JMJD2B antagonizes histone H3 Lys9 tri-methylation at pericentric heterochromatin (10). JMJD2C, also known as GASC1, is amplified in squamous cell carcinomas and metastatic lung carcinoma, and inhibition of JMJD2C expression decreases cell proliferation (11,12). JMJD2C has also been identified as a downstream target of Oct-4 and is critical for the regulation of self-renewal in embryonic stem cells (13).

1. Kubicek, S. et al. (2006) Ernst Schering Res Found Workshop , 1-27.
2. Lin, W. and Dent, S.Y. (2006) Curr Opin Genet Dev 16, 137-42.
3. Klose, R.J. et al. (2006) Nat Rev Genet 7, 715-27.
4. Chen, Z. et al. (2007) Proc Natl Acad Sci USA 104, 10818-23.
5. Lee, J. et al. (2008) Nat Struct Mol Biol 15, 109-11.
6. Whetstine, J.R. et al. (2006) Cell 125, 467-81.
7. Shin, S. and Janknecht, R. (2007) Biochem Biophys Res Commun 359, 742-6.
8. Gray, S.G. et al. (2005) J Biol Chem 280, 28507-18.
9. Zhang, D. et al. (2005) Mol Cell Biol 25, 6404-14.
10. Fodor, B.D. et al. (2006) Genes Dev 20, 1557-62.
11. Cloos, P.A. et al. (2006) Nature 442, 307-11.
12. Italiano, A. et al. (2006) Cancer Genet Cytogenet 167, 122-30.
13. Loh, Y.H. et al. (2007) Genes Dev 21, 2545-57.

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JMJD2B Antibody

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