Phosphorylation Is a Central Mechanism for Circadian Control of Metabolism and Physiology

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Phosphorylation Is a Central Mechanism for Circadian Control of Metabolism and Physiology. / Robles, Maria S; Humphrey, Sean J; Mann, Matthias.

In: Cell Metabolism, Vol. 25, No. 1, 10.01.2017, p. 118-127.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Robles, MS, Humphrey, SJ & Mann, M 2017, 'Phosphorylation Is a Central Mechanism for Circadian Control of Metabolism and Physiology', Cell Metabolism, vol. 25, no. 1, pp. 118-127. https://doi.org/10.1016/j.cmet.2016.10.004

APA

Robles, M. S., Humphrey, S. J., & Mann, M. (2017). Phosphorylation Is a Central Mechanism for Circadian Control of Metabolism and Physiology. Cell Metabolism, 25(1), 118-127. https://doi.org/10.1016/j.cmet.2016.10.004

Vancouver

Robles MS, Humphrey SJ, Mann M. Phosphorylation Is a Central Mechanism for Circadian Control of Metabolism and Physiology. Cell Metabolism. 2017 Jan 10;25(1):118-127. https://doi.org/10.1016/j.cmet.2016.10.004

Author

Robles, Maria S ; Humphrey, Sean J ; Mann, Matthias. / Phosphorylation Is a Central Mechanism for Circadian Control of Metabolism and Physiology. In: Cell Metabolism. 2017 ; Vol. 25, No. 1. pp. 118-127.

Bibtex

@article{7f2b0c17c873409da6d126164c7fae3c,
title = "Phosphorylation Is a Central Mechanism for Circadian Control of Metabolism and Physiology",
abstract = "Circadian clocks are self-sustainable endogenous oscillators, present in virtually every cell, driving daily cycles of metabolism and physiology. The molecular mechanism of the circadian clock is based on interconnected transcriptional and translational feedback loops. While many studies have addressed circadian rhythms of the transcriptome and, to a lesser extent, the proteome, none have investigated the phosphoproteome. We apply mass spectrometry-based phosphoproteomics to obtain the first global in vivo quantification of circadian phosphorylation in mammals. Of more than 20,000 phosphosites, 25% significantly oscillate in the mouse liver, including novel sites on core clock proteins. The extent and amplitude of phosphorylation cycles far exceeds those observed in RNA and protein abundance. Our data indicate a dominant regulatory role for phosphorylation-dependent circadian tuning of signaling pathways. This allows the organism to integrate different signals and rapidly and economically respond to daily changes in nutrient availability and physiological states.",
keywords = "Amino Acid Sequence, Animals, CLOCK Proteins, Circadian Clocks, Circadian Rhythm, Enzyme Activation, Female, Liver, Male, Metabolic Networks and Pathways, Mice, Mice, Inbred C57BL, Models, Biological, Phosphoproteins, Phosphorylation, Protein Kinases, Proteome, Signal Transduction, Time Factors, Journal Article",
author = "Robles, {Maria S} and Humphrey, {Sean J} and Matthias Mann",
note = "Copyright {\textcopyright} 2017 Elsevier Inc. All rights reserved.",
year = "2017",
month = jan,
day = "10",
doi = "10.1016/j.cmet.2016.10.004",
language = "English",
volume = "25",
pages = "118--127",
journal = "Cell Metabolism",
issn = "1550-4131",
publisher = "Cell Press",
number = "1",

}

RIS

TY - JOUR

T1 - Phosphorylation Is a Central Mechanism for Circadian Control of Metabolism and Physiology

AU - Robles, Maria S

AU - Humphrey, Sean J

AU - Mann, Matthias

N1 - Copyright © 2017 Elsevier Inc. All rights reserved.

PY - 2017/1/10

Y1 - 2017/1/10

N2 - Circadian clocks are self-sustainable endogenous oscillators, present in virtually every cell, driving daily cycles of metabolism and physiology. The molecular mechanism of the circadian clock is based on interconnected transcriptional and translational feedback loops. While many studies have addressed circadian rhythms of the transcriptome and, to a lesser extent, the proteome, none have investigated the phosphoproteome. We apply mass spectrometry-based phosphoproteomics to obtain the first global in vivo quantification of circadian phosphorylation in mammals. Of more than 20,000 phosphosites, 25% significantly oscillate in the mouse liver, including novel sites on core clock proteins. The extent and amplitude of phosphorylation cycles far exceeds those observed in RNA and protein abundance. Our data indicate a dominant regulatory role for phosphorylation-dependent circadian tuning of signaling pathways. This allows the organism to integrate different signals and rapidly and economically respond to daily changes in nutrient availability and physiological states.

AB - Circadian clocks are self-sustainable endogenous oscillators, present in virtually every cell, driving daily cycles of metabolism and physiology. The molecular mechanism of the circadian clock is based on interconnected transcriptional and translational feedback loops. While many studies have addressed circadian rhythms of the transcriptome and, to a lesser extent, the proteome, none have investigated the phosphoproteome. We apply mass spectrometry-based phosphoproteomics to obtain the first global in vivo quantification of circadian phosphorylation in mammals. Of more than 20,000 phosphosites, 25% significantly oscillate in the mouse liver, including novel sites on core clock proteins. The extent and amplitude of phosphorylation cycles far exceeds those observed in RNA and protein abundance. Our data indicate a dominant regulatory role for phosphorylation-dependent circadian tuning of signaling pathways. This allows the organism to integrate different signals and rapidly and economically respond to daily changes in nutrient availability and physiological states.

KW - Amino Acid Sequence

KW - Animals

KW - CLOCK Proteins

KW - Circadian Clocks

KW - Circadian Rhythm

KW - Enzyme Activation

KW - Female

KW - Liver

KW - Male

KW - Metabolic Networks and Pathways

KW - Mice

KW - Mice, Inbred C57BL

KW - Models, Biological

KW - Phosphoproteins

KW - Phosphorylation

KW - Protein Kinases

KW - Proteome

KW - Signal Transduction

KW - Time Factors

KW - Journal Article

U2 - 10.1016/j.cmet.2016.10.004

DO - 10.1016/j.cmet.2016.10.004

M3 - Journal article

C2 - 27818261

VL - 25

SP - 118

EP - 127

JO - Cell Metabolism

JF - Cell Metabolism

SN - 1550-4131

IS - 1

ER -

ID: 184324188