Lysine Deacetylases and Regulated Glycolysis in Macrophages

Publication date: Available online 19 March 2018
Source:Trends in Immunology
Author(s): Melanie R. Shakespear, Abishek Iyer, Catherine Youting Cheng, Kaustav Das Gupta, Amit Singhal, David P. Fairlie, Matthew J. Sweet
Regulated cellular metabolism has emerged as a fundamental process controlling macrophage functions, but there is still much to uncover about the precise signaling mechanisms involved. Lysine acetylation regulates the activity, stability, and/or localization of metabolic enzymes, as well as inflammatory responses, in macrophages. Two protein families, the classical zinc-dependent histone deacetylases (HDACs) and the NAD-dependent HDACs (sirtuins, SIRTs), mediate lysine deacetylation. We describe here mechanisms by which classical HDACs and SIRTs directly regulate specific glycolytic enzymes, as well as evidence that links these protein deacetylases to the regulation of glycolysis-related genes. In these contexts, we discuss HDACs and SIRTs as key control points for regulating immunometabolism and inflammatory outputs from macrophages.



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