Background
The reversible lysine acetylation of histones and non-histone proteins is a crucial post-translational modification that regulates diverse cellular processes, including chromatin dynamics, gene expression, cell cycle progression, apoptosis, differentiation, DNA replication, DNA repair, nuclear import, and neuronal repression. More than 20 acetyltransferases and 18 histone deacetylases (HDACs) have been identified, but the mechanisms governing substrate selection and site specificity of these enzymes remain unclear. Dysregulation of protein acetylation has been implicated in the development of cancers and other diseases, and HDACs have become likely targets for anti-cancer drugs.
Cellular location
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