Uncoupling the Mitogenic and Metabolic Functions of FGF1 by Tuning FGF1-FGF Receptor Dimer Stability

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 c...
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Autor*in:	Zhifeng Huang [verfasserIn] Florian Atger [verfasserIn] Loïc Dayon [verfasserIn] Antonio Núñez Galindo [verfasserIn] Jingkui Wang [verfasserIn] Eva Martin [verfasserIn] Laetitia Da Silva [verfasserIn] Ivan Montoliu [verfasserIn] Sebastiano Collino [verfasserIn] Francois-Pierre Martin [verfasserIn] Joanna Ratajczak [verfasserIn] Carles Cantó [verfasserIn] Martin Kussmann [verfasserIn] Felix Naef [verfasserIn] Frédéric Gachon [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2017

Schlagwörter:	circadian clock acetylation liver metabolism SIRT3 NAD+ SILAC proteomics

Übergeordnetes Werk:	In: Cell Reports - Elsevier, 2015, 20(2017), 7, Seite 1717-1728
Übergeordnetes Werk:	volume:20 ; year:2017 ; number:7 ; pages:1717-1728

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.1016/j.celrep.2017.06.063

Katalog-ID:	DOAJ055369715

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520			\|a 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.
650		4	\|a circadian clock
650		4	\|a acetylation
650		4	\|a liver metabolism
650		4	\|a SIRT3
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650		4	\|a SILAC proteomics
653		0	\|a Biology (General)
700	0		\|a Florian Atger \|e verfasserin \|4 aut
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700	0		\|a Antonio Núñez Galindo \|e verfasserin \|4 aut
700	0		\|a Jingkui Wang \|e verfasserin \|4 aut
700	0		\|a Eva Martin \|e verfasserin \|4 aut
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700	0		\|a Felix Naef \|e verfasserin \|4 aut
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allfields	10.1016/j.celrep.2017.06.063 doi (DE-627)DOAJ055369715 (DE-599)DOAJ3aa9c1bfec0b4f3d81065c8e401a3545 DE-627 ger DE-627 rakwb eng QH301-705.5 Zhifeng Huang verfasserin aut Uncoupling the Mitogenic and Metabolic Functions of FGF1 by Tuning FGF1-FGF Receptor Dimer Stability 2017 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier 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. circadian clock acetylation liver metabolism SIRT3 NAD+ SILAC proteomics Biology (General) Florian Atger verfasserin aut Loïc Dayon verfasserin aut Antonio Núñez Galindo verfasserin aut Jingkui Wang verfasserin aut Eva Martin verfasserin aut Laetitia Da Silva verfasserin aut Ivan Montoliu verfasserin aut Sebastiano Collino verfasserin aut Francois-Pierre Martin verfasserin aut Joanna Ratajczak verfasserin aut Carles Cantó verfasserin aut Martin Kussmann verfasserin aut Felix Naef verfasserin aut Frédéric Gachon verfasserin aut In Cell Reports Elsevier, 2015 20(2017), 7, Seite 1717-1728 (DE-627)684964562 (DE-600)2649101-1 22111247 nnns volume:20 year:2017 number:7 pages:1717-1728 https://doi.org/10.1016/j.celrep.2017.06.063 kostenfrei https://doaj.org/article/3aa9c1bfec0b4f3d81065c8e401a3545 kostenfrei http://www.sciencedirect.com/science/article/pii/S2211124717310586 kostenfrei https://doaj.org/toc/2211-1247 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2110 GBV_ILN_2112 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 20 2017 7 1717-1728
spelling	10.1016/j.celrep.2017.06.063 doi (DE-627)DOAJ055369715 (DE-599)DOAJ3aa9c1bfec0b4f3d81065c8e401a3545 DE-627 ger DE-627 rakwb eng QH301-705.5 Zhifeng Huang verfasserin aut Uncoupling the Mitogenic and Metabolic Functions of FGF1 by Tuning FGF1-FGF Receptor Dimer Stability 2017 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier 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. circadian clock acetylation liver metabolism SIRT3 NAD+ SILAC proteomics Biology (General) Florian Atger verfasserin aut Loïc Dayon verfasserin aut Antonio Núñez Galindo verfasserin aut Jingkui Wang verfasserin aut Eva Martin verfasserin aut Laetitia Da Silva verfasserin aut Ivan Montoliu verfasserin aut Sebastiano Collino verfasserin aut Francois-Pierre Martin verfasserin aut Joanna Ratajczak verfasserin aut Carles Cantó verfasserin aut Martin Kussmann verfasserin aut Felix Naef verfasserin aut Frédéric Gachon verfasserin aut In Cell Reports Elsevier, 2015 20(2017), 7, Seite 1717-1728 (DE-627)684964562 (DE-600)2649101-1 22111247 nnns volume:20 year:2017 number:7 pages:1717-1728 https://doi.org/10.1016/j.celrep.2017.06.063 kostenfrei https://doaj.org/article/3aa9c1bfec0b4f3d81065c8e401a3545 kostenfrei http://www.sciencedirect.com/science/article/pii/S2211124717310586 kostenfrei https://doaj.org/toc/2211-1247 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2110 GBV_ILN_2112 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 20 2017 7 1717-1728
allfields_unstemmed	10.1016/j.celrep.2017.06.063 doi (DE-627)DOAJ055369715 (DE-599)DOAJ3aa9c1bfec0b4f3d81065c8e401a3545 DE-627 ger DE-627 rakwb eng QH301-705.5 Zhifeng Huang verfasserin aut Uncoupling the Mitogenic and Metabolic Functions of FGF1 by Tuning FGF1-FGF Receptor Dimer Stability 2017 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier 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. circadian clock acetylation liver metabolism SIRT3 NAD+ SILAC proteomics Biology (General) Florian Atger verfasserin aut Loïc Dayon verfasserin aut Antonio Núñez Galindo verfasserin aut Jingkui Wang verfasserin aut Eva Martin verfasserin aut Laetitia Da Silva verfasserin aut Ivan Montoliu verfasserin aut Sebastiano Collino verfasserin aut Francois-Pierre Martin verfasserin aut Joanna Ratajczak verfasserin aut Carles Cantó verfasserin aut Martin Kussmann verfasserin aut Felix Naef verfasserin aut Frédéric Gachon verfasserin aut In Cell Reports Elsevier, 2015 20(2017), 7, Seite 1717-1728 (DE-627)684964562 (DE-600)2649101-1 22111247 nnns volume:20 year:2017 number:7 pages:1717-1728 https://doi.org/10.1016/j.celrep.2017.06.063 kostenfrei https://doaj.org/article/3aa9c1bfec0b4f3d81065c8e401a3545 kostenfrei http://www.sciencedirect.com/science/article/pii/S2211124717310586 kostenfrei https://doaj.org/toc/2211-1247 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2110 GBV_ILN_2112 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 20 2017 7 1717-1728
allfieldsGer	10.1016/j.celrep.2017.06.063 doi (DE-627)DOAJ055369715 (DE-599)DOAJ3aa9c1bfec0b4f3d81065c8e401a3545 DE-627 ger DE-627 rakwb eng QH301-705.5 Zhifeng Huang verfasserin aut Uncoupling the Mitogenic and Metabolic Functions of FGF1 by Tuning FGF1-FGF Receptor Dimer Stability 2017 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier 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. circadian clock acetylation liver metabolism SIRT3 NAD+ SILAC proteomics Biology (General) Florian Atger verfasserin aut Loïc Dayon verfasserin aut Antonio Núñez Galindo verfasserin aut Jingkui Wang verfasserin aut Eva Martin verfasserin aut Laetitia Da Silva verfasserin aut Ivan Montoliu verfasserin aut Sebastiano Collino verfasserin aut Francois-Pierre Martin verfasserin aut Joanna Ratajczak verfasserin aut Carles Cantó verfasserin aut Martin Kussmann verfasserin aut Felix Naef verfasserin aut Frédéric Gachon verfasserin aut In Cell Reports Elsevier, 2015 20(2017), 7, Seite 1717-1728 (DE-627)684964562 (DE-600)2649101-1 22111247 nnns volume:20 year:2017 number:7 pages:1717-1728 https://doi.org/10.1016/j.celrep.2017.06.063 kostenfrei https://doaj.org/article/3aa9c1bfec0b4f3d81065c8e401a3545 kostenfrei http://www.sciencedirect.com/science/article/pii/S2211124717310586 kostenfrei https://doaj.org/toc/2211-1247 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2110 GBV_ILN_2112 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 20 2017 7 1717-1728
allfieldsSound	10.1016/j.celrep.2017.06.063 doi (DE-627)DOAJ055369715 (DE-599)DOAJ3aa9c1bfec0b4f3d81065c8e401a3545 DE-627 ger DE-627 rakwb eng QH301-705.5 Zhifeng Huang verfasserin aut Uncoupling the Mitogenic and Metabolic Functions of FGF1 by Tuning FGF1-FGF Receptor Dimer Stability 2017 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier 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. circadian clock acetylation liver metabolism SIRT3 NAD+ SILAC proteomics Biology (General) Florian Atger verfasserin aut Loïc Dayon verfasserin aut Antonio Núñez Galindo verfasserin aut Jingkui Wang verfasserin aut Eva Martin verfasserin aut Laetitia Da Silva verfasserin aut Ivan Montoliu verfasserin aut Sebastiano Collino verfasserin aut Francois-Pierre Martin verfasserin aut Joanna Ratajczak verfasserin aut Carles Cantó verfasserin aut Martin Kussmann verfasserin aut Felix Naef verfasserin aut Frédéric Gachon verfasserin aut In Cell Reports Elsevier, 2015 20(2017), 7, Seite 1717-1728 (DE-627)684964562 (DE-600)2649101-1 22111247 nnns volume:20 year:2017 number:7 pages:1717-1728 https://doi.org/10.1016/j.celrep.2017.06.063 kostenfrei https://doaj.org/article/3aa9c1bfec0b4f3d81065c8e401a3545 kostenfrei http://www.sciencedirect.com/science/article/pii/S2211124717310586 kostenfrei https://doaj.org/toc/2211-1247 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2110 GBV_ILN_2112 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 20 2017 7 1717-1728
language	English
source	In Cell Reports 20(2017), 7, Seite 1717-1728 volume:20 year:2017 number:7 pages:1717-1728
sourceStr	In Cell Reports 20(2017), 7, Seite 1717-1728 volume:20 year:2017 number:7 pages:1717-1728
format_phy_str_mv	Article
institution	findex.gbv.de
topic_facet	circadian clock acetylation liver metabolism SIRT3 NAD+ SILAC proteomics Biology (General)
isfreeaccess_bool	true
container_title	Cell Reports
authorswithroles_txt_mv	Zhifeng Huang @@aut@@ Florian Atger @@aut@@ Loïc Dayon @@aut@@ Antonio Núñez Galindo @@aut@@ Jingkui Wang @@aut@@ Eva Martin @@aut@@ Laetitia Da Silva @@aut@@ Ivan Montoliu @@aut@@ Sebastiano Collino @@aut@@ Francois-Pierre Martin @@aut@@ Joanna Ratajczak @@aut@@ Carles Cantó @@aut@@ Martin Kussmann @@aut@@ Felix Naef @@aut@@ Frédéric Gachon @@aut@@
publishDateDaySort_date	2017-01-01T00:00:00Z
hierarchy_top_id	684964562
id	DOAJ055369715
language_de	englisch
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callnumber-first	Q - Science
author	Zhifeng Huang
spellingShingle	Zhifeng Huang misc QH301-705.5 misc circadian clock misc acetylation misc liver metabolism misc SIRT3 misc NAD+ misc SILAC proteomics misc Biology (General) Uncoupling the Mitogenic and Metabolic Functions of FGF1 by Tuning FGF1-FGF Receptor Dimer Stability
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topic_title	QH301-705.5 Uncoupling the Mitogenic and Metabolic Functions of FGF1 by Tuning FGF1-FGF Receptor Dimer Stability circadian clock acetylation liver metabolism SIRT3 NAD+ SILAC proteomics
topic	misc QH301-705.5 misc circadian clock misc acetylation misc liver metabolism misc SIRT3 misc NAD+ misc SILAC proteomics misc Biology (General)
topic_unstemmed	misc QH301-705.5 misc circadian clock misc acetylation misc liver metabolism misc SIRT3 misc NAD+ misc SILAC proteomics misc Biology (General)
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title	Uncoupling the Mitogenic and Metabolic Functions of FGF1 by Tuning FGF1-FGF Receptor Dimer Stability
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title_full	Uncoupling the Mitogenic and Metabolic Functions of FGF1 by Tuning FGF1-FGF Receptor Dimer Stability
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author_browse	Zhifeng Huang Florian Atger Loïc Dayon Antonio Núñez Galindo Jingkui Wang Eva Martin Laetitia Da Silva Ivan Montoliu Sebastiano Collino Francois-Pierre Martin Joanna Ratajczak Carles Cantó Martin Kussmann Felix Naef Frédéric Gachon
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title_sort	uncoupling the mitogenic and metabolic functions of fgf1 by tuning fgf1-fgf receptor dimer stability
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title_auth	Uncoupling the Mitogenic and Metabolic Functions of FGF1 by Tuning FGF1-FGF Receptor Dimer Stability
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.
abstractGer	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.
abstract_unstemmed	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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title_short	Uncoupling the Mitogenic and Metabolic Functions of FGF1 by Tuning FGF1-FGF Receptor Dimer Stability
url	https://doi.org/10.1016/j.celrep.2017.06.063 https://doaj.org/article/3aa9c1bfec0b4f3d81065c8e401a3545 http://www.sciencedirect.com/science/article/pii/S2211124717310586 https://doaj.org/toc/2211-1247
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author2Str	Florian Atger Loïc Dayon Antonio Núñez Galindo Jingkui Wang Eva Martin Laetitia Da Silva Ivan Montoliu Sebastiano Collino Francois-Pierre Martin Joanna Ratajczak Carles Cantó Martin Kussmann Felix Naef Frédéric Gachon
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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. 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