Lysine acetylation,a more prevalent posttranslational regulation of protein function

Acetylation of proteins on lysine residues,including non-histones lysine acetylation,is a prevalent and reversible posttranslational modification.Technological limitations in this field have long impeded the progress in analysis of lysine acetylation′s cellular roles.In the past several years,however,quite a number of non-histones lysine acetylation have been brought to light,largely due to the maturation of detection technologies such as high-resolution mass spectrometry and label-free quantification(LFQ).Although the molecular mechanisms underlying cellular regulation of lysine acetylation remain elusive and the detection of highly dynamic lysine acetylation is still a challenge,mounting documented evidence has demonstrated that lysine acetylation is widely involved in such cellular biological activities as cell growth,apoptosis,cytokinetics and cell metabolisms.In this review,we present the progression in this field as well as our current understanding of this modification,starting with the developing detection technologies of lysine acetylation.We also highlight the function of lysine acetylation in the regulation of gene transcription,energy metabolism,cancer development as well as its therapeutic implications.