The functional diversity of protein lysine methylation.
The functional diversity of protein lysine methylation.
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DOI:
10.1002/msb.134974
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发表时间:
2014-04-08
影响因子:
9.9
通讯作者:
Couture, Jean-Francois
中科院分区:
文献类型:
--
作者:
Lanouette, Sylvain;Mongeon, Vanessa;Figeys, Daniel;Couture, Jean-Francois
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.
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作者:
Barbier M;Owings JP;Martínez-Ramos I;Damron FH;Gomila R;Blázquez J;Goldberg JB;Albertí S
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