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A quantitative map of the liver mitochondrial phosphoproteome reveals posttranslational control of ketogenesis.

Publication ,  Journal Article
Grimsrud, PA; Carson, JJ; Hebert, AS; Hubler, SL; Niemi, NM; Bailey, DJ; Jochem, A; Stapleton, DS; Keller, MP; Westphall, MS; Yandell, BS ...
Published in: Cell Metab
November 7, 2012

Mitochondria are dynamic organelles that play a central role in a diverse array of metabolic processes. Elucidating mitochondrial adaptations to changing metabolic demands and the pathogenic alterations that underlie metabolic disorders represent principal challenges in cell biology. Here, we performed multiplexed quantitative mass spectrometry-based proteomics to chart the remodeling of the mouse liver mitochondrial proteome and phosphoproteome during both acute and chronic physiological transformations in more than 50 mice. Our analyses reveal that reversible phosphorylation is widespread in mitochondria, and is a key mechanism for regulating ketogenesis during the onset of obesity and type 2 diabetes. Specifically, we have demonstrated that phosphorylation of a conserved serine on Hmgcs2 (S456) significantly enhances its catalytic activity in response to increased ketogenic demand. Collectively, our work describes the plasticity of this organelle at high resolution and provides a framework for investigating the roles of proteome restructuring and reversible phosphorylation in mitochondrial adaptation.

Duke Scholars

Published In

Cell Metab

DOI

EISSN

1932-7420

Publication Date

November 7, 2012

Volume

16

Issue

5

Start / End Page

672 / 683

Location

United States

Related Subject Headings

  • Tandem Mass Spectrometry
  • Proteomics
  • Proteome
  • Phosphorylation
  • Phosphopeptides
  • Mitochondria, Liver
  • Mice, Obese
  • Mice
  • Ketone Bodies
  • Hydroxymethylglutaryl-CoA Synthase
 

Citation

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Chicago
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MLA
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Grimsrud, P. A., Carson, J. J., Hebert, A. S., Hubler, S. L., Niemi, N. M., Bailey, D. J., … Pagliarini, D. J. (2012). A quantitative map of the liver mitochondrial phosphoproteome reveals posttranslational control of ketogenesis. Cell Metab, 16(5), 672–683. https://doi.org/10.1016/j.cmet.2012.10.004
Grimsrud, Paul A., Joshua J. Carson, Alex S. Hebert, Shane L. Hubler, Natalie M. Niemi, Derek J. Bailey, Adam Jochem, et al. “A quantitative map of the liver mitochondrial phosphoproteome reveals posttranslational control of ketogenesis.Cell Metab 16, no. 5 (November 7, 2012): 672–83. https://doi.org/10.1016/j.cmet.2012.10.004.
Grimsrud PA, Carson JJ, Hebert AS, Hubler SL, Niemi NM, Bailey DJ, et al. A quantitative map of the liver mitochondrial phosphoproteome reveals posttranslational control of ketogenesis. Cell Metab. 2012 Nov 7;16(5):672–83.
Grimsrud, Paul A., et al. “A quantitative map of the liver mitochondrial phosphoproteome reveals posttranslational control of ketogenesis.Cell Metab, vol. 16, no. 5, Nov. 2012, pp. 672–83. Pubmed, doi:10.1016/j.cmet.2012.10.004.
Grimsrud PA, Carson JJ, Hebert AS, Hubler SL, Niemi NM, Bailey DJ, Jochem A, Stapleton DS, Keller MP, Westphall MS, Yandell BS, Attie AD, Coon JJ, Pagliarini DJ. A quantitative map of the liver mitochondrial phosphoproteome reveals posttranslational control of ketogenesis. Cell Metab. 2012 Nov 7;16(5):672–683.
Journal cover image

Published In

Cell Metab

DOI

EISSN

1932-7420

Publication Date

November 7, 2012

Volume

16

Issue

5

Start / End Page

672 / 683

Location

United States

Related Subject Headings

  • Tandem Mass Spectrometry
  • Proteomics
  • Proteome
  • Phosphorylation
  • Phosphopeptides
  • Mitochondria, Liver
  • Mice, Obese
  • Mice
  • Ketone Bodies
  • Hydroxymethylglutaryl-CoA Synthase