Abstract
The potential for developing therapeutics for cancers driven by aberrant gene expression is becoming a reality in recent years, largely due to the identification and characterization of the enzymatic components regulating chromatin structure and function. One of the major classes of chromatin-modifying enzymes is the histone methyltransferases. These enzymes catalyze the methylation of lysine and arginine residues on the core nucleosomal histones. The methylation pattern present on the histones is associated with different chromatin states depending upon the particular site of methylation. The lysine and arginine methyltransferases (KMTs and RMTs) comprise enzyme families with promising therapeutic potential because they have been found to be altered in diseases with high unmet need (e.g., cancer) and are amenable to small molecule drug discovery efforts (Copeland et al., Nat Rev Drug Discov 8(9):724–732, 2009). The purpose of this chapter is to review the histone lysine and arginine methyltransferases with particular focus on their histone substrates and their association with cancer and status of the development of small molecule inhibitors.
Richard Chesworth and Tim J. Wigle contributed equally to the chapter.
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Acknowledgement
We thank Dr. Robert A. Copeland for helpful discussions and careful reading of the Chapter.
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Chesworth, R., Wigle, T.J., Kuntz, K.W., Smith, J.J., Richon, V.M. (2014). Histone Methyltransferases: Opportunities in Cancer Drug Discovery. In: Lübbert, M., Jones, P. (eds) Epigenetic Therapy of Cancer. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-38404-2_9
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