Background
Acetylation of lysine, like phosphorylation of serine, threonine or tyrosine, is an important
reversible modification controlling protein activity. The conserved amino-terminal domains of
the four core histones (H2A, H2B, H3, and H4) contain lysines that are acetylated by histone
acetyltransferases (HATs) and deacetylated by histone deacetylases (HDACs) (PMID:
9667866). Signaling resulting in acetylation/deacetylation of histones, transcription factors,
and other proteins affects a diverse array of cellular processes including chromatin structure
and gene activity, cell growth, differentiation, and apoptosis (PMID: 14593721). Recent
proteomic surveys suggest that acetylation of lysine residues may be a widespread and
important form of post-translational protein modification that affects thousands of proteins
involved in control of cell cycle and metabolism, longevity, actin polymerization, and nuclear
transport (PMID: 19608861). The regulation of protein acetylation status is impaired in
cancer and polyglutamine diseases (PMID: 11864588), and HDACs have become promising
targets for anti-cancer drugs currently in development (PMID: 15032670)
