Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation

Amelia J. Still; Brendan J. Floyd; Alexander S. Hebert; Craig A. Bingman; Joshua J. Carson; Drew R. Gunderson; Brendan K. Dolan; Paul A. Grimsrud; Kristin E. Dittenhafer-Reed; Donald S. Stapleton; Mark P. Keller; Michael S. Westphall; John M. Denu; Alan D. Attie; Joshua J. Coon; David J. Pagliarini

doi:10.1074/jbc.M113.483396

Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation

Amelia J. Still, Brendan J. Floyd, Alexander S. Hebert, Craig A. Bingman, Joshua J. Carson, Drew R. Gunderson, Brendan K. Dolan, Paul A. Grimsrud, Kristin E. Dittenhafer-Reed, Donald S. Stapleton, Mark P. Keller, Michael S. Westphall, John M. Denu, Alan D. Attie, Joshua J. Coon, David J. Pagliarini

Research output: Contribution to journal › Article › peer-review

73 Scopus citations

Abstract

Background: Lysine acetylation, a prevalent post-translational modification, alters mitochondrial metabolism in response to nutrient changes. Results: Quantitative proteomics distinguishes dynamic and static acetylation sites, highlighting 48 likely regulatory sites of thousands identified. Conclusion: Acetylation of Acat1 lysine 260, a highly dynamic site, reversibly inhibits enzyme activity. Significance: Quantitative, state-specific proteomic analyses accelerate the functional characterization of acetylation in mitochondrial remodeling.

Original language	English
Pages (from-to)	26209-26219
Number of pages	11
Journal	Journal of Biological Chemistry
Volume	288
Issue number	36
DOIs	https://doi.org/10.1074/jbc.M113.483396
State	Published - Sep 6 2013
Externally published	Yes

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Still, A. J., Floyd, B. J., Hebert, A. S., Bingman, C. A., Carson, J. J., Gunderson, D. R., Dolan, B. K., Grimsrud, P. A., Dittenhafer-Reed, K. E., Stapleton, D. S., Keller, M. P., Westphall, M. S., Denu, J. M., Attie, A. D., Coon, J. J., & Pagliarini, D. J. (2013). Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation. Journal of Biological Chemistry, 288(36), 26209-26219. https://doi.org/10.1074/jbc.M113.483396

Still, Amelia J. ; Floyd, Brendan J. ; Hebert, Alexander S. ; Bingman, Craig A. ; Carson, Joshua J. ; Gunderson, Drew R. ; Dolan, Brendan K. ; Grimsrud, Paul A. ; Dittenhafer-Reed, Kristin E. ; Stapleton, Donald S. ; Keller, Mark P. ; Westphall, Michael S. ; Denu, John M. ; Attie, Alan D. ; Coon, Joshua J. ; Pagliarini, David J. / Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation. In: Journal of Biological Chemistry. 2013 ; Vol. 288, No. 36. pp. 26209-26219.

@article{696da356d9cf4374a08f7c02adcad2dd,

title = "Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation",

abstract = "Background: Lysine acetylation, a prevalent post-translational modification, alters mitochondrial metabolism in response to nutrient changes. Results: Quantitative proteomics distinguishes dynamic and static acetylation sites, highlighting 48 likely regulatory sites of thousands identified. Conclusion: Acetylation of Acat1 lysine 260, a highly dynamic site, reversibly inhibits enzyme activity. Significance: Quantitative, state-specific proteomic analyses accelerate the functional characterization of acetylation in mitochondrial remodeling.",

author = "Still, {Amelia J.} and Floyd, {Brendan J.} and Hebert, {Alexander S.} and Bingman, {Craig A.} and Carson, {Joshua J.} and Gunderson, {Drew R.} and Dolan, {Brendan K.} and Grimsrud, {Paul A.} and Dittenhafer-Reed, {Kristin E.} and Stapleton, {Donald S.} and Keller, {Mark P.} and Westphall, {Michael S.} and Denu, {John M.} and Attie, {Alan D.} and Coon, {Joshua J.} and Pagliarini, {David J.}",

year = "2013",

month = sep,

day = "6",

doi = "10.1074/jbc.M113.483396",

language = "English",

volume = "288",

pages = "26209--26219",

journal = "Journal of Biological Chemistry",

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Still, AJ, Floyd, BJ, Hebert, AS, Bingman, CA, Carson, JJ, Gunderson, DR, Dolan, BK, Grimsrud, PA, Dittenhafer-Reed, KE, Stapleton, DS, Keller, MP, Westphall, MS, Denu, JM, Attie, AD, Coon, JJ & Pagliarini, DJ 2013, 'Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation', Journal of Biological Chemistry, vol. 288, no. 36, pp. 26209-26219. https://doi.org/10.1074/jbc.M113.483396

Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation. / Still, Amelia J.; Floyd, Brendan J.; Hebert, Alexander S.; Bingman, Craig A.; Carson, Joshua J.; Gunderson, Drew R.; Dolan, Brendan K.; Grimsrud, Paul A.; Dittenhafer-Reed, Kristin E.; Stapleton, Donald S.; Keller, Mark P.; Westphall, Michael S.; Denu, John M.; Attie, Alan D.; Coon, Joshua J.; Pagliarini, David J.

In: Journal of Biological Chemistry, Vol. 288, No. 36, 06.09.2013, p. 26209-26219.

Research output: Contribution to journal › Article › peer-review

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AU - Still, Amelia J.

AU - Floyd, Brendan J.

AU - Hebert, Alexander S.

AU - Bingman, Craig A.

AU - Carson, Joshua J.

AU - Gunderson, Drew R.

AU - Dolan, Brendan K.

AU - Grimsrud, Paul A.

AU - Dittenhafer-Reed, Kristin E.

AU - Stapleton, Donald S.

AU - Keller, Mark P.

AU - Westphall, Michael S.

AU - Denu, John M.

AU - Attie, Alan D.

AU - Coon, Joshua J.

AU - Pagliarini, David J.

PY - 2013/9/6

Y1 - 2013/9/6

N2 - Background: Lysine acetylation, a prevalent post-translational modification, alters mitochondrial metabolism in response to nutrient changes. Results: Quantitative proteomics distinguishes dynamic and static acetylation sites, highlighting 48 likely regulatory sites of thousands identified. Conclusion: Acetylation of Acat1 lysine 260, a highly dynamic site, reversibly inhibits enzyme activity. Significance: Quantitative, state-specific proteomic analyses accelerate the functional characterization of acetylation in mitochondrial remodeling.

AB - Background: Lysine acetylation, a prevalent post-translational modification, alters mitochondrial metabolism in response to nutrient changes. Results: Quantitative proteomics distinguishes dynamic and static acetylation sites, highlighting 48 likely regulatory sites of thousands identified. Conclusion: Acetylation of Acat1 lysine 260, a highly dynamic site, reversibly inhibits enzyme activity. Significance: Quantitative, state-specific proteomic analyses accelerate the functional characterization of acetylation in mitochondrial remodeling.

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