Journal
CELL
Volume 146, Issue 4, Pages 607-620Publisher
CELL PRESS
DOI: 10.1016/j.cell.2011.06.050
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Funding
- U.S. Army [DAMD17-02-1-0403]
- National Institute of Aging [R37-012859]
- National Institutes of Health (NIH) [DK070299, GM47467, 5P01CA120964-03]
- National Institute of Neurological Disorders and Stroke [1F31NS057872-01]
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Previous experiments suggest a connection between the N-alpha-acetylation of proteins and sensitivity of cells to apoptotic signals. Here, we describe a biochemical assay to detect the acetylation status of proteins and demonstrate that protein N-alpha-acetylation is regulated by the availability of acetylCoA. Because the antiapoptotic protein Bcl-xL is known to influence mitochondrial metabolism, we reasoned that Bcl-xL may provide a link between protein N-alpha-acetylation and apoptosis. Indeed, Bcl-xL overexpression leads to a reduction in levels of acetyl-CoA and N-alpha-acetylated proteins in the cell. This effect is independent of Bax and Bak, the known binding partners of Bcl-xL. Increasing cellular levels of acetyl-CoA by addition of acetate or citrate restores protein N-alpha-acetylation in Bcl-xL-expressing cells and confers sensitivity to apoptotic stimuli. We propose that acetyl-CoA serves as a signaling molecule that couples apoptotic sensitivity to metabolism by regulating protein N-alpha-acetylation.
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