SIRT3 deacetylates ATP synthase F1 complex proteins in response to nutrient- and exercise-induced stress.
AUTHORS
Vassilopoulos
AAthanassios ,
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
- PMCID: PMC4085980.
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.