TY - JOUR
T1 - Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation
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.
UR - http://www.scopus.com/inward/record.url?scp=84883659304&partnerID=8YFLogxK
U2 - 10.1074/jbc.M113.483396
DO - 10.1074/jbc.M113.483396
M3 - Article
C2 - 23864654
AN - SCOPUS:84883659304
SN - 0021-9258
VL - 288
SP - 26209
EP - 26219
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 36
ER -