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SIRT3 deacetylates ATP synthase F1 complex proteins in response to nutrient- and exercise-induced stress.

Authors

Vassilopoulos A Athanassios , Pennington JD J Daniel , Andresson T Thorkell , Rees DM David M , Bosley AD Allen D , Fearnley IM Ian M , Ham A Amy , Flynn CR Charles Robb , Hill S Salisha , Rose KL Kristie Lindsey , Kim HS Hyun-Seok , Deng CX Chu-Xia , Walker JE John E , Gius D David .
Antioxidants & redox signaling. 2014 8 1; 21(4).
551-64

Abstract

Adenosine triphosphate (ATP) synthase uses chemiosmotic energy across the inner mitochondrial membrane to convert adenosine diphosphate and orthophosphate into ATP, whereas genetic deletion of Sirt3 decreases mitochondrial ATP levels. Here, we investigate the mechanistic connection between SIRT3 and energy homeostasis.

Adenosine triphosphate (ATP) synthase uses chemiosmotic energy across the inner mitochondrial membrane to convert adenosine diphosphate and orthophosphate into ATP, whereas genetic deletion of Sirt3 decreases mitochondrial ATP levels. Here, we investigate the mechanistic connection between SIRT3 and energy homeostasis.