Lysine acetylation: Codified crosstalk with other posttranslational modifications

被引：777

作者：

Yang, Xiang-Jiao ^{[1
,2
]}

Seto, Edward ^{[3
]}

机构：

[1] McGill Univ, Dept Med, Mol Oncol Grp, Ctr Hlth, Montreal, PQ H3A 1A1, Canada

[2] McGill Canc Ctr, Montreal, PQ H3A 1A1, Canada

[3] Univ S Florida, Coll Med, H Lee Moffitt Canc Ctr & Res Inst, Mol Oncol Program, Tampa, FL 33612 USA

来源：

MOLECULAR CELL | 2008年 / 31卷 / 04期

基金：

美国国家卫生研究院; 加拿大健康研究院;

关键词：

D O I：

10.1016/j.molcel.2008.07.002

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Lysine acetylation has emerged as a major posttranslational modification for histones. Crossregulation between this and other modifications is crucial in modulating chromatin-based transcriptional control and shaping inheritable epigenetic programs. In addition to histones, many other nuclear proteins and various cytoplasmic regulators are subject to lysine acetylation. This review focuses on recent findings pertinent to acetylation of nonhistone proteins and emphasizes how this modification might crosstalk with phosphorylation, methylation, ubiquitination, sumoylation, and others to form code-like multisite modification programs for dynamic control of cellular signaling under diverse conditions.

引用

页码：449 / 461

页数：13

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