Lysine methylation： beyond histones

• Published in: Acta biochimica et biophysica Sinica Vol. 44; no. 1; pp. 14 - 27
• Main Authors: Zhang, Xi, Wen, Hong, Shi, Xiaobing
• Format: Journal Article
• Language: English
• Published: China Oxford University Press 2012
• Subjects: Acetylation; Animals; Histone Demethylases - metabolism; Histone-Lysine N-Methyltransferase - metabolism; Humans; Lysine - metabolism; Methylation; Methyltransferases - metabolism; Mice; Protein Methyltransferases - metabolism; Protein Processing, Post-Translational; Tumor Suppressor Protein p53 - metabolism; 乙酰化; 甲基化; 组蛋白密码; 翻译后修饰; 蛋白磷酸化; 蛋白质相互作用; 赖氨酸; 非组蛋白; lysine methyltransferase (KMT); lysine demethylase (KDM); methylation; epigenetics; p53
• ISSN: 1672-9145; 1745-7270; 1745-7270
• DOI: 10.1093/abbs/gmr100

Posttranslational modifications （PTMs） of histone proteins, such as acetylation, methylation, phosphorylation, and ubiquitylation, play essential roles in regulating chromatin dynamics. Combinations of different modifications on the histone proteins, termed ＇histone code＇ in many cases, extend the information potential of the genetic code by regulating DNA at the epigenetic level. Many PTMs occur on non-histone proteins as well as histones, regulating protein-protein interactions, stability, localization, and/or enzymatic activities of proteins involved in diverse cellular processes. Although protein phosphorylation, ubiquitylation, and acetylation have been extensively studied, only a few proteins other than histones have been reported that can be modified by lysine methylation. This review summarizes the current progress on lysine methylation of non- histone proteins, and we propose that lysine methylation, like phosphorylation and acetylation, is a common PTM that regulates proteins in diverse cellular processes.