Deacetylation of p53 induces autophagy by suppressing bmf expression Academic Article uri icon


MeSH Major

  • Adaptor Proteins, Signal Transducing
  • Autophagy
  • Gene Expression
  • Protein Processing, Post-Translational
  • Tumor Suppressor Protein p53


  • Interferon γ (IFN-γ)-induced cell death is mediated by the BH3-only domain protein, Bik, in a p53-independent manner. However, the effect of IFN-γ on p53 and how this affects autophagy have not been reported. The present study demonstrates that IFN-γ down-regulated expression of the BH3 domain-only protein, Bmf, in human and mouse airway epithelial cells in a p53-dependent manner. p53 also suppressed Bmf expression in response to other cell death-stimulating agents, including ultraviolet radiation and histone deacetylase inhibitors. IFN-γ did not affect Bmf messenger RNA half-life but increased nuclear p53 levels and the interaction of p53 with the Bmf promoter. IFN-γ-induced interaction of HDAC1 and p53 resulted in the deacetylation of p53 and suppression of Bmf expression independent of p53's proline-rich domain. Suppression of Bmf facilitated IFN-γ-induced autophagy by reducing the interaction of Beclin-1 and Bcl-2. Furthermore, autophagy was prominent in cultured bmf(-/-) but not in bmf(+/+) cells. Collectively, these observations show that deacetylation of p53 suppresses Bmf expression and facilitates autophagy.

publication date

  • April 2013



  • Academic Article



  • eng

PubMed Central ID

  • PMC3639396

Digital Object Identifier (DOI)

  • 10.1083/jcb.201205064

PubMed ID

  • 23629966

Additional Document Info

start page

  • 427

end page

  • 37


  • 201


  • 3