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Cell. 2011 Aug 19;146(4):607-20. doi: 10.1016/j.cell.2011.06.050.

Metabolic regulation of protein N-alpha-acetylation by Bcl-xL promotes cell survival.

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  • 1Department of Cell Biology, Beth Israel Deaconess Medical Center, Boston, MA 02115, USA.

Abstract

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 acetyl-CoA. 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.

Copyright © 2011 Elsevier Inc. All rights reserved.

PMID:
21854985
[PubMed - indexed for MEDLINE]
PMCID:
PMC3182480
Free PMC Article
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