The functional diversity of protein lysine methylation
Article first published online: 8 APR 2014
© 2014 The Authors. Published under the terms of the CC BY license.
This is an open access article under the terms of the Creative Commons Attribution 4.0 License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
Molecular Systems Biology
Volume 10, Issue 4, April 2014
How to Cite
Mol Syst Biol. (2014) 10: 724
- Issue published online: 4 APR 2014
- Article first published online: 8 APR 2014
- Manuscript Accepted: 18 FEB 2014
- Manuscript Revised: 17 FEB 2014
- Manuscript Received: 8 NOV 2013
- Canadian Institutes for Health Research. Grant Number: GMX-209406
- Natural Sciences and Engineering Research Council of Canada. Grant Number: 191666
- Fonds de Recherche en Santé du Québec (FRSQ)
- lysine demethylation;
- lysine methylation;
- systems biology
Large-scale characterization of post-translational modifications (PTMs), such as phosphorylation, acetylation and ubiquitination, has highlighted their importance in the regulation of a myriad of signaling events. While high-throughput technologies have tremendously helped cataloguing the proteins modified by these PTMs, the identification of lysine-methylated proteins, a PTM involving the transfer of one, two or three methyl groups to the ε-amine of a lysine side chain, has lagged behind. While the initial findings were focused on the methylation of histone proteins, several studies have recently identified novel non-histone lysine-methylated proteins. This review provides a compilation of all lysine methylation sites reported to date. We also present key examples showing the impact of lysine methylation and discuss the circuitries wired by this important PTM.