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Mol Cell. 2008 Aug 22;31(4):449-61. doi: 10.1016/j.molcel.2008.07.002.

Lysine acetylation: codified crosstalk with other posttranslational modifications.

Author information

1
Molecular Oncology Group, Department of Medicine, McGill University Health Centre, Montréal, QC H3A1A1, Canada. xiang-jiao.yang@mcgill.ca

Abstract

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.

PMID:
18722172
PMCID:
PMC2551738
DOI:
10.1016/j.molcel.2008.07.002
[Indexed for MEDLINE]
Free PMC Article

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