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
Couture, Jean-Francois
中科院分区:
生物学1区
文献类型:
--
作者:
Lanouette, Sylvain;Mongeon, Vanessa;Figeys, Daniel;Couture, Jean-Francois

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翻译后修饰(PTM)的大规模表征,如磷酸化,乙酰化和泛素化,突出了它们在调节无数信号事件中的重要性。虽然高通量技术极大地帮助了这些PTM修饰的蛋白质的编目,但赖氨酸甲基化蛋白质的鉴定,涉及将一个,两个或三个甲基转移到赖氨酸侧链的ε-胺的PTM,已经落后。虽然最初的发现集中在组蛋白的甲基化,但最近有几项研究发现了新的非组蛋白赖氨酸甲基化蛋白。这篇评论提供了迄今为止报道的所有赖氨酸甲基化位点的汇编。我们还提出了关键的例子显示赖氨酸甲基化的影响,并讨论了这个重要的PTM布线电路。
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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期刊: mBio
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