Lysine acetylation: codified crosstalk with other posttranslational modifications

Mol Cell. 2008 Aug 22;31(4):449-461. doi: 10.1016/j.molcel.2008.07.002.


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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Acetylation
  • Acetyltransferases / metabolism
  • Amidohydrolases / metabolism
  • Amino Acid Sequence
  • Animals
  • Humans
  • Lysine / metabolism*
  • Molecular Sequence Data
  • Nuclear Proteins / chemistry
  • Nuclear Proteins / metabolism
  • Protein Processing, Post-Translational*


  • Nuclear Proteins
  • Acetyltransferases
  • Amidohydrolases
  • Lysine