Metabolic regulation of protein N-alpha-acetylation by Bcl-xL promotes cell survival Academic Article uri icon


MeSH Major

  • Cell Survival
  • Proteins
  • bcl-X Protein


  • 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.

publication date

  • August 19, 2011



  • Academic Article



  • eng

PubMed Central ID

  • PMC3182480

Digital Object Identifier (DOI)

  • 10.1016/j.cell.2011.06.050

PubMed ID

  • 21854985

Additional Document Info

start page

  • 607

end page

  • 20


  • 146


  • 4