The epithelial-mesenchymal transition (EMT) is a vital driver of
tumor progression. It is a well-known and complex trans-differentiation process in which epithelial cells undergo morphogenetic changes with loss of apical-basal polarity, but acquire spindle-shaped mesenchymal phenotypes.
Lysine acetylation is a type of
protein modification that favors reversibly altering the structure and function of target molecules via the modulation of
lysine acetyltransferases (KATs), as well as
lysine deacetylases (KDACs). To date, research has found that
histones and non-
histone proteins can be acetylated to facilitate EMT. Interestingly,
histone acetylation is a type of epigenetic regulation that is capable of modulating the acetylation levels of distinct
histones at the promoters of EMT-related markers, EMT-inducing
transcription factors (EMT-TFs), and EMT-related long non-coding RNAs to control EMT. However, non-
histone acetylation is a post-translational modification, and its effect on EMT mainly relies on modulating the acetylation of EMT marker
proteins, EMT-TFs, and EMT-related signal transduction molecules. In addition, several inhibitors against KATs and KDACs have been developed, some of which can suppress the development of different
cancers by targeting EMT. In this review, we discuss the complex biological roles and molecular mechanisms underlying
histone acetylation and non-
histone protein acetylation in the control of EMT, highlighting
lysine acetylation as potential strategy for the treatment of
cancer through the regulation of EMT. Video Abstract.