期刊
MOLECULAR CELL
卷 31, 期 4, 页码 449-461出版社
CELL PRESS
DOI: 10.1016/j.molcel.2008.07.002
关键词
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资金
- National Institutes of Health
- American Heart Association
- Kaul Foundation
- Canadian Institutes of Health Research
- National Cancer Institute of Canada
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.
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