biostudies-literatureAli INational Institute of Allergy and Infectious DiseasesAmfAR Institute for HIV Cure ResearchNational Institute of Diabetes and Digestive and Kidney DiseasesNIDDK NIH HHSNIDA NIH HHSNIA NIH HHSNIAID NIH HHSUniversity of California, San FranciscoAmerican Society for MicrobiologyNational Institute on Drug AbuseNIGMS NIH HHSNational Institute on Aging1216-1252https://www.ebi.ac.uk/biostudies/studies/S-EPMC6609103biostudies-literatureUnknown118(3)Post-translational acetylation of lysine residues has emerged as a key regulatory mechanism in all eukaryotic organisms. Originally discovered in 1963 as a unique modification of histones, acetylation marks are now found on thousands of nonhistone proteins located in virtually every cellular compartment. Here we summarize key findings in the field of protein acetylation over the past 20 years with a focus on recent discoveries in nuclear, cytoplasmic, and mitochondrial compartments. Collectively, these findings have elevated protein acetylation as a major post-translational modification, underscoring its physiological relevance in gene regulation, cell signaling, metabolism, and disease.Chemical reviewsLysine Acetylation Goes Global: From Epigenetics to Metabolism and Therapeutics.PMC6609103R21 AG051111P30 AI0277631DP1DA038043DP1 DA038043T32 AI007334R01 AI083139R01 DA043142R01DA0431425R24 DK085610-06T32 GM007175R01AI083139-06R24 DK085610R21AG051111Ali IConrad RJOtt MVerdin EfalseLysine Acetylation Goes Global: From Epigenetics to Metabolism and Therapeutics.Post-translational acetylation of lysine residues has emerged as a key regulatory mechanism in all eukaryotic organisms. Originally discovered in 1963 as a unique modification of histones, acetylation marks are now found on thousands of nonhistone proteins located in virtually every cellular compartment. Here we summarize key findings in the field of protein acetylation over the past 20 years with a focus on recent discoveries in nuclear, cytoplasmic, and mitochondrial compartments. Collectively, these findings have elevated protein acetylation as a major post-translational modification, underscoring its physiological relevance in gene regulation, cell signaling, metabolism, and disease.2018-01-01T00:00:00Z2018 Feb2024-11-21T03:27:28.702Z2019-07-25T07:03:46ZS-EPMC66091032940570710.1021/acs.chemrev.7b00181