Regulation of Fatty Acid Oxidation by Reversible Lysine Acetylation

Recently it was discovered that as many as 20 percent of all mitochondrial proteins are subject to reversible acetylation on surface lysines. Nothing is known about the acetylation mechanism. In this grant-supported project, it is hypothesized that fatty acid oxidation is the primary source of acetyl groups used for protein acetylation in mitochondria. This is being tested in vitro by culturing cells in the presence of radiolabeled energy substrates and studying the resulting pattern of labeling on mitochondrial proteins. Mouse models are used for in vivo studies that link the rate of fatty acid oxidation and intra-mitochondrial levels of acetyl-CoA to protein acetylation.

Functional studies will be done to compare the efficiency of fatty acid oxidation between tissues with high levels of mitochondrial protein acetylation and those with low levels of acetylation. It is predicted that increasing levels of acetylation are associated with a decline in fatty acid oxidation efficiency.

Source(s) of Support
UPMC Health System Competitive Medical Research Fund

Principal Investigator
Eric Goetzman,PhD

Last Update
August 14, 2010
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Last Update
August 14, 2010