The emerging field of dynamic lysine methylation of non-histone proteins

被引：217

作者：

Huang, Jing ^{[1
]}

Berger, Shelley L. ^{[1
]}

机构：

[1] Wistar Inst Anat & Biol, Gene Express & Regulat Program, Philadelphia, PA 19087 USA

来源：

CURRENT OPINION IN GENETICS & DEVELOPMENT | 2008年 / 18卷 / 02期

关键词：

D O I：

10.1016/j.gde.2008.01.012

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

Post-translational modifications (PTMs) regulate protein structure and function. Lysine methylation abundantly decorates histone proteins and has recently been detected on non-histone proteins. In particular, the tumor suppressor and transcription factor p53 has provided a model for lysine methylation on a non-histone protein. As found for histones, lysine methylation is dynamic and can be reversed by demethylation. Lysine methylation regulates function via several distinct mechanisms. Methyl lysine provides docking sites for binding of effector proteins. Methylation can serve to inhibit alternate PTMs on the same lysine residue. In addition, lysine can be monomethylated, dimethylated, or trimethylated, and these levels of methylation correlate with distinct genomic locations and functions. Taking into account combinatorial activity with numerous other PTMs, lysine methylation provides enormous functional diversity and regulatory complexity.

引用

页码：152 / 158

页数：7

共 47 条

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