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Critical roles of non-histone protein lysine methylation in human tumorigenesis
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Critical roles of non-histone protein lysine methylation in human tumorigenesis
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Journal Article
Critical roles of non-histone protein lysine methylation in human tumorigenesis
2015
Overview
Key Points
Lysine methylation is widely recognized as a fundamental post-translational modification.
Most protein lysine methyltransferases (PKMTs) contain the SET domain, but several non-SET proteins such as DOT1-like histone H3 lysine 79 methyltransferase (DOT1L), methyltransferase-like 10 (METTL10) and METTL21A are also known to have lysine
N
-methyltransferase activity.
Protein lysine demethylases (PKDMs) consist of the lysine-specific demethylase 1 (LSD1) family, which are flavin-dependent monoamine oxidases, and the Jumonji C (JmjC) domain-containing proteins, which are α-ketoglutarate-dependent Fe(ii) dioxygenases.
The biological importance of protein lysine methylation in cancer can be categorized into five different functions: effect on other protein modifications; protein–protein interactions; protein stability; subcellular localization; and promoter binding.
Although the most widely recognized function of PKMTs and PKDMs in cancer is their effects on histones and epigenetic regulation, nearly 20 non-histone proteins related to human cancer, including p53 and RB1, have also been discovered to be methylated at lysine residues.
Somatic mutations of PKMTs and PKDMs are frequently found in human cancer, and it is possible that they may affect the methylation of non-histone substrates.
Inhibitors targeting PKMTs and PKDMs are considered to be promising agents for anticancer therapy, and it is important that a thorough understanding of all of the substrates of these enzymes is made to discern the precise mechanism of action of these inhibitors.
Although dysregulation of histone methylation has been widely studied in cancer, accumulating evidence suggests that cancer-relevant non-histone proteins such as p53, RB1 and signal transducer and activator of transcription 3 (STAT3) are also regulated by lysine methylation. This Review summarizes the possible functions of non-histone protein lysine methylation in cancer.
Several protein lysine methyltransferases and demethylases have been identified to have critical roles in histone modification. A large body of evidence has indicated that their dysregulation is involved in the development and progression of various diseases, including cancer, and these enzymes are now considered to be potential therapeutic targets. Although most studies have focused on histone methylation, many reports have revealed that these enzymes also regulate the methylation dynamics of non-histone proteins such as p53, RB1 and STAT3 (signal transducer and activator of transcription 3), which have important roles in human tumorigenesis. In this Review, we summarize the molecular functions of protein lysine methylation and its involvement in human cancer, with a particular focus on lysine methylation of non-histone proteins.
Publisher
Nature Publishing Group UK,Nature Publishing Group
Subject
