Regulation of Cellular Metabolism by Protein Lysine Acetylation

Citations Over TimeTop 1% of 2010 papers

Abstract

Protein lysine acetylation has emerged as a key posttranslational modification in cellular regulation, in particular through the modification of histones and nuclear transcription regulators. We show that lysine acetylation is a prevalent modification in enzymes that catalyze intermediate metabolism. Virtually every enzyme in glycolysis, gluconeogenesis, the tricarboxylic acid (TCA) cycle, the urea cycle, fatty acid metabolism, and glycogen metabolism was found to be acetylated in human liver tissue. The concentration of metabolic fuels, such as glucose, amino acids, and fatty acids, influenced the acetylation status of metabolic enzymes. Acetylation activated enoyl-coenzyme A hydratase/3-hydroxyacyl-coenzyme A dehydrogenase in fatty acid oxidation and malate dehydrogenase in the TCA cycle, inhibited argininosuccinate lyase in the urea cycle, and destabilized phosphoenolpyruvate carboxykinase in gluconeogenesis. Our study reveals that acetylation plays a major role in metabolic regulation.

Related Papers

• → Acetylome analysis reveals the involvement of lysine acetylation in diverse biological processes in Phytophthora sojae(2016)41 cited
• → A Method to Determine Lysine Acetylation Stoichiometries(2014)38 cited
• → Versatility of ARD1/NAA10-mediated protein lysine acetylation(2018)16 cited
• → Site-Specific Quantification of Lysine Acetylation Using Isotopic Labeling(2017)8 cited
• → Measurement and Analysis of Lysine Acetylation by KAT Complexes In Vitro and In Vivo(2019)3 cited