Lysine Acetylation of Proteins and Its Characterization in Human Systems
Posttranslational acetylation modifications of proteins have important consequences for cell biology, including effects on protein trafficking and cellular localization as well as on the interactions of acetylated proteins with other proteins and macromolecules such as DNA. Experiments to uncover and characterize protein acetylation events have historically been more challenging than investigating another common posttranslational modification, protein phosphorylation. More recently, high-quality antibodies that recognize acetylated lysine residues present in acetylated proteins and improved proteomic methodologies have facilitated the discovery that acetylation occurs on numerous cellular proteins and allowed characterization of the dynamics and functional effects of many acetylation events. This article summarizes some established biochemical information about how protein acetylation takes place and is regulated, in order to lay the foundation for subsequent descriptions of strategies used by our lab and others either to directly study acetylation of an individual factor or to identify groups of proteins targeted for acetylation that can then be examined in isolation.
KeywordsPosttranslational modifications Acetyltransferases Histone deacetylases Sirtuins Immunodetection Proteomics Bromodomain
This work was supported by NIH grants R01 AG027258 and R01 AG026534 as well as by the Department of Toxicology and Cancer Biology of the University of Kentucky College of Medicine.
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