Functions and mechanisms of non-histone protein acetylation

Ne-lysine acetylationwas discovered more than half a century ago as a post-translational modification of histonesand has been extensively studied in the context of transcription regulation. In the past decade, proteomic analyses have revealed that non-histone proteinsare frequently acetylatedand constitute a major portion of the acetylome in mammalian cells. Indeed, non-histone protein acetylationis involved in key cellular processes relevant to physiology and disease, such as gene transcription, DNA damage repair, cell division, signal transduction, protein folding, autophagy and metabolism. Acetylationaffects protein functions through diverse mechanisms, including by regulating protein stability, enzymatic activity, subcellular localizationand crosstalk with other post-translational modifications and by controlling protein–protein and protein–DNA interactions. In this Review, we discuss recent progress in our understanding of the scope, functional diversity and mechanisms of non-histone protein acetylation.