期刊
CELL REPORTS
卷 20, 期 7, 页码 1729-1743出版社
CELL PRESS
DOI: 10.1016/j.celrep.2017.07.065
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资金
- wiss National Science Foundation [31003A-153340, 310030-173079]
- Ecole Polytechnique Federale de Lausanne
- Novartis Foundation for Medical-Biological Research [16C213]
- European Research Council [ERC-2010-StG-260988]
- Leenaards Foundation
- Swiss National Science Foundation (SNF) [31003A_153340] Funding Source: Swiss National Science Foundation (SNF)
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.
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