Abstract
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.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 4257-4272 |
| Number of pages | 16 |
| Journal | Cellular and Molecular Life Sciences |
| Volume | 72 |
| Issue number | 22 |
| DOIs | |
| State | Published - Nov 1 2015 |
Funding
We apologize to researchers whose papers are not cited here because of space constraints. We thank Briana Dennehey and Raquel Jaeger for critical reading of this paper. This work is supported in part by grants from the Welch Foundation (G1719), American Cancer Society (RSG-13-290-01-TBE), and CPRIT (RP110471 and RP140323). Xiaobing Shi is a member of the scientific advisory board of EpiCypher Inc and is a MD Anderson Cancer Center R. Lee Clark Fellow.
Keywords
- ERα
- G9a
- Lysine methylation
- SETD7
- SMYD2
- p53
ASJC Scopus subject areas
- Molecular Medicine
- Molecular Biology
- Pharmacology
- Cellular and Molecular Neuroscience
- Cell Biology