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Cell Rep. 2017 Aug 15;20(7):1729-1743. doi: 10.1016/j.celrep.2017.07.065.

Circadian and Feeding Rhythms Orchestrate the Diurnal Liver Acetylome.

Author information

1
Diabetes and Circadian Rhythms Department, Nestlé Institute of Health Sciences, 1015 Lausanne, Switzerland; Institute of Bioengineering, School of Life Sciences, Ecole Polytechnique Fédérale de Lausanne, 1015 Lausanne, Switzerland.
2
Diabetes and Circadian Rhythms Department, Nestlé Institute of Health Sciences, 1015 Lausanne, Switzerland; Department of Pharmacology and Toxicology, University of Lausanne, 1015 Lausanne, Switzerland.
3
Systems Nutrition, Metabonomics & Proteomics, Nestlé Institute of Health Sciences, 1015 Lausanne, Switzerland.
4
Institute of Bioengineering, School of Life Sciences, Ecole Polytechnique Fédérale de Lausanne, 1015 Lausanne, Switzerland.
5
Diabetes and Circadian Rhythms Department, Nestlé Institute of Health Sciences, 1015 Lausanne, Switzerland.
6
Diabetes and Circadian Rhythms Department, Nestlé Institute of Health Sciences, 1015 Lausanne, Switzerland; School of Life Sciences, Ecole Polytechnique Fédérale Lausanne, 1015 Lausanne, Switzerland.
7
Diabetes and Circadian Rhythms Department, Nestlé Institute of Health Sciences, 1015 Lausanne, Switzerland; School of Life Sciences, Ecole Polytechnique Fédérale Lausanne, 1015 Lausanne, Switzerland. Electronic address: frederic.gachon@rd.nestle.com.

Abstract

Lysine acetylation is involved in various biological processes and is considered a key reversible post-translational modification in the regulation of gene expression, enzyme activity, and subcellular localization. This post-translational modification is therefore highly relevant in the context of circadian biology, but its characterization on the proteome-wide scale and its circadian clock dependence are still poorly described. Here, we provide a comprehensive and rhythmic acetylome map of the mouse liver. Rhythmic acetylated proteins showed subcellular localization-specific phases that correlated with the related metabolites in the regulated pathways. Mitochondrial proteins were over-represented among the rhythmically acetylated proteins and were highly correlated with SIRT3-dependent deacetylation. SIRT3 activity being nicotinamide adenine dinucleotide (NAD)+ level-dependent, we show that NAD+ is orchestrated by both feeding rhythms and the circadian clock through the NAD+ salvage pathway but also via the nicotinamide riboside pathway. Hence, the diurnal acetylome relies on a functional circadian clock and affects important diurnal metabolic pathways in the mouse liver.

KEYWORDS:

NAD(+); SILAC proteomics; SIRT3; acetylation; circadian clock; liver metabolism

PMID:
28813682
PMCID:
PMC5568034
DOI:
10.1016/j.celrep.2017.07.065
[Indexed for MEDLINE]
Free PMC Article

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