Kristin E. Dittenhafer-Reed

TL;DR: This work developed and applied a quantitative mass spectrometry method to probe the liver mitochondrial acetyl-proteome during CR versus control diet in mice that were wild-type or lacked the protein deacetylase SIRT3, and revealed widespread reprogramming of mitochondrial protein acetylation in response to CR.

TL;DR: Findings show SIRT3 regulates ketone body production during fasting and provide molecular insight into how protein acetylation can regulate enzymatic activity.

TL;DR: This work provides direct biochemical and biological evidence establishing an exquisite regulatory relationship between IDH2 and SIRT3 under acute and chronic caloric restriction, and implicates Sirt3 as a potential regulator of IDH 2-dependent functions in cancer cell metabolism.

TL;DR: The current understanding of the chemistry of catalysis, biological targets, and endogenous regulation of sirtuin activity is reviewed, and recent efforts to generate small-molecule regulators of sIRTuin activity are discussed.

TL;DR: Evidence that SIRT3 impacts ketone body utilization in the brain is provided and a pivotal role for Sirt3 is revealed in the coordination between tissues required for metabolic homeostasis in order to reduce the acetate load on mitochondrial proteins.