The functional diversity of protein lysine methylation.
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.
Ottawa Institute of Systems Biology, Department of Biochemistry, Microbiology and Immunology, University of Ottawa, Ottawa, Canada.
Sylvain
S
Lanouette
Vanessa
V
Mongeon
Daniel
D
Figeys
Jean-François
JF
Couture
D000107:Acetylation; D000595:Amino Acid Sequence; D006657:Histones / Q000235:genetics / Q000378:metabolism*; D008239:Lysine / Q000378:metabolism*; D008745:Methylation; D011499:Protein Processing, Post-Translational / Q000235:genetics*; D011506:Proteins / Q000235:genetics / Q000378:metabolism*; D049490:Systems Biology; D054875:Ubiquitination / Q000235:genetics
D006657:Histones; D011506:Proteins; D008239:Lysine