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 journalArticlepeer-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 languageEnglish
Pages (from-to)26209-26219
Number of pages11
JournalJournal of Biological Chemistry
Volume288
Issue number36
DOIs
StatePublished - Sep 6 2013
Externally publishedYes

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