Lysine acetylation: codified crosstalk with other posttranslational modifications.
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.
Yang
Xiang-Jiao
XJ
Molecular Oncology Group, Department of Medicine, McGill University Health Centre, Montréal, QC H3A 1A1, Canada; McGill Cancer Centre, Montréal, QC H3A 1A1, Canada. Electronic address: xiang-jiao.yang@mcgill.ca.
Seto
Edward
E
Molecular Oncology Program, H. Lee Moffitt Cancer Center and Research Institute, Tampa, FL 33612, USA. Electronic address: ed.seto@moffitt.org.
D000107:Acetylation; D000123:Acetyltransferases / Q000378:metabolism; D000581:Amidohydrolases / Q000378:metabolism; D000595:Amino Acid Sequence; D000818:Animals; D006801:Humans; D008239:Lysine / Q000378:metabolism*; D008969:Molecular Sequence Data; D009687:Nuclear Proteins / Q000737:chemistry / Q000378:metabolism; D011499:Protein Processing, Post-Translational
D009687:Nuclear Proteins; D000123:Acetyltransferases; D000581:Amidohydrolases; D008239:Lysine