Emerging roles of lysine methylation on non-histone proteins

• Published in: Cellular and molecular life sciences : CMLS Vol. 72; no. 22; pp. 4257 - 4272
• Main Authors: Zhang, Xi, Huang, Yaling, Shi, Xiaobing
• Format: Journal Article
• Language: English
• Published: Basel Springer Basel 01.11.2015; Springer Nature B.V
• Subjects: Amino acids; Animals; Biochemistry; Biomedical and Life Sciences; Biomedicine; Cell Biology; Chromatin; Epigenetics; Estrogen Receptor alpha - metabolism; Estrogen receptors; Estrogens; Eukaryotes; Gene regulation; Histone-Lysine N-Methyltransferase - metabolism; Histones; Histones - metabolism; Humans; Life Sciences; Lysine; Lysine - metabolism; Methylation; Models, Biological; Molecular biology; Nuclear receptors; p53 Protein; Protein Processing, Post-Translational; Proteins; Receptors; Review; Tumor Suppressor Protein p53 - metabolism; SMYD2; Lysine methylation; ERα; G9a; SETD7; p53
• ISSN: 1420-682X; 1420-9071
• DOI: 10.1007/s00018-015-2001-4

Lysine methylation is a common posttranslational modification (PTM) of histones that is important for the epigenetic regulation of transcription and chromatin in eukaryotes. Increasing evidence demonstrates that in addition to histones, lysine methylation also occurs on various non-histone proteins, especially transcription- and chromatin-regulating proteins. In this review, we will briefly describe the histone lysine methyltransferases (KMTs) that have a broad spectrum of non-histone substrates. We will use p53 and nuclear receptors, especially estrogen receptor alpha, as examples to discuss the dynamic nature of non-histone protein lysine methylation, the writers, erasers, and readers of these modifications, and the crosstalk between lysine methylation and other PTMs in regulating the functions of the modified proteins. Understanding the roles of lysine methylation in normal cells and during development will shed light on the complex biology of diseases associated with the dysregulation of lysine methylation on both histones and non-histone proteins.