The functional diversity of protein lysine methylation
Abstract 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 p...
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| Format: | Article |
| Language: | English |
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Springer Nature
2014-04-01
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| Series: | Molecular Systems Biology |
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| Online Access: | https://doi.org/10.1002/msb.134974 |
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| _version_ | 1849738813799137280 |
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| author | Sylvain Lanouette Vanessa Mongeon Daniel Figeys Jean‐François Couture |
| author_facet | Sylvain Lanouette Vanessa Mongeon Daniel Figeys Jean‐François Couture |
| author_sort | Sylvain Lanouette |
| collection | DOAJ |
| description | Abstract 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. |
| format | Article |
| id | doaj-art-3bde2bd8de554055bd9f038d74c6e7d8 |
| institution | DOAJ |
| issn | 1744-4292 |
| language | English |
| publishDate | 2014-04-01 |
| publisher | Springer Nature |
| record_format | Article |
| series | Molecular Systems Biology |
| spelling | doaj-art-3bde2bd8de554055bd9f038d74c6e7d82025-08-20T03:06:27ZengSpringer NatureMolecular Systems Biology1744-42922014-04-0110412610.1002/msb.134974The functional diversity of protein lysine methylationSylvain Lanouette0Vanessa Mongeon1Daniel Figeys2Jean‐François Couture3Ottawa Institute of Systems Biology, Department of Biochemistry, Microbiology and Immunology, University of OttawaOttawa Institute of Systems Biology, Department of Biochemistry, Microbiology and Immunology, University of OttawaOttawa Institute of Systems Biology, Department of Biochemistry, Microbiology and Immunology, University of OttawaOttawa Institute of Systems Biology, Department of Biochemistry, Microbiology and Immunology, University of OttawaAbstract 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.https://doi.org/10.1002/msb.134974lysine demethylationlysine methylationnetworksproteomicssystems biology |
| spellingShingle | Sylvain Lanouette Vanessa Mongeon Daniel Figeys Jean‐François Couture The functional diversity of protein lysine methylation Molecular Systems Biology lysine demethylation lysine methylation networks proteomics systems biology |
| title | 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_short | The functional diversity of protein lysine methylation |
| title_sort | functional diversity of protein lysine methylation |
| topic | lysine demethylation lysine methylation networks proteomics systems biology |
| url | https://doi.org/10.1002/msb.134974 |
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