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 m...
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| Format: | Online |
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European Molecular Biology Organization
2014
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| Online Access: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4023394/ |
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pubmed-40233942014-05-16 The functional diversity of protein lysine methylation Lanouette, Sylvain Mongeon, Vanessa Figeys, Daniel Couture, Jean‐François Review 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. European Molecular Biology Organization 2014-04-08 /pmc/articles/PMC4023394/ /pubmed/24714364 http://dx.doi.org/10.1002/msb.134974 Text en © 2014 EMBO This is an open access article under the terms of the Creative Commons Attribution 4.0 (http://creativecommons.org/licenses/by/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. |
| repository_type |
Open Access Journal |
| institution_category |
Foreign Institution |
| institution |
US National Center for Biotechnology Information |
| building |
NCBI PubMed |
| collection |
Online Access |
| language |
English |
| format |
Online |
| author |
Lanouette, Sylvain Mongeon, Vanessa Figeys, Daniel Couture, Jean‐François |
| spellingShingle |
Lanouette, Sylvain Mongeon, Vanessa Figeys, Daniel Couture, Jean‐François The functional diversity of protein lysine methylation |
| author_facet |
Lanouette, Sylvain Mongeon, Vanessa Figeys, Daniel Couture, Jean‐François |
| author_sort |
Lanouette, Sylvain |
| title |
The functional diversity of protein lysine methylation |
| title_short |
The functional diversity of protein lysine methylation |
| title_full |
The functional diversity of protein lysine methylation |
| title_fullStr |
The functional diversity of protein lysine methylation |
| title_full_unstemmed |
The functional diversity of protein lysine methylation |
| title_sort |
functional diversity of protein lysine methylation |
| description |
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. |
| publisher |
European Molecular Biology Organization |
| publishDate |
2014 |
| url |
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4023394/ |
| _version_ |
1612090001103781888 |