Regulation of cellular metabolism by protein lysine acetylation Zhao, S. et al. Science 327, 1000–1004 (2010)
Lys acetylation in the nucleus modifies histones and regulators of transcription. To investigate the non-nuclear functions of protein acetylation, Zhao et al. analyzed the mitochondrial and cytosolic fractions of human liver tissues by tandem liquid chromatography–tandem mass spectrometry. They found that almost every enzyme involved in glycolysis, gluconeogenesis, the tricarboxylic acid cycle, the urea cycle, fatty acid metabolism and glycogen metabolism is acetylated. The acetylation status of the enzymes they investigated further is regulated by the concentration of metabolic fuels, and the acetylation status regulates enzyme activity. For example, the acetylation and activity of enoyl CoA hydratase–3-hydroxyacyl CoA, which catalyzes two steps in fatty acid oxidation, increases in the presence of fatty acids. Thus, in response to metabolic fuels, Lys acetylation regulates the activity of enzymes that catalyze cellular metabolism.
This is a preview of subscription content, access via your institution
