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SIRT1 regulates autoacetylation and histone acetyltransferase activity of TIP60

Jiadong Wang1, Junjie Chen

  • 1Department of Experimental Radiation Oncology, University of Texas M. D. Anderson Cancer Center, Houston, Texas 77030, USA.

The Journal of Biological Chemistry
|January 27, 2010
PubMed

Insights

The histone acetyltransferase TIP60 is activated by autoacetylation after UV damage, enhancing its DNA repair functions. SIRT1 negatively regulates this process, revealing a key control mechanism for TIP60 activity.

Area of Science:

  • Molecular biology
  • Cancer research
  • Epigenetics

Background:

  • The histone acetyltransferase TIP60 is crucial for apoptosis induction after UV radiation.
  • TIP60 is frequently lost in human carcinomas, highlighting its role in cancer suppression.

Purpose of the Study:

  • To elucidate the regulatory mechanisms of TIP60 activation in response to UV-induced DNA damage.
  • To identify factors that control TIP60's histone acetyltransferase activity.

Main Methods:

  • Investigated TIP60 autoacetylation following UV exposure.
  • Analyzed the effect of autoacetylation on TIP60 oligomerization and substrate interaction.
  • Identified and characterized the deacetylase activity of SIRT1 on TIP60.

Main Results:

  • TIP60 undergoes autoacetylation upon UV damage, which is essential for its activation.
  • Autoacetylation promotes TIP60 oligomer dissociation and enhances substrate binding.
  • SIRT1 was identified as a specific deacetylase that inhibits TIP60 activity in vivo.

Conclusions:

  • TIP60 autoacetylation is a critical regulatory step controlling its activity in DNA damage response.
  • The interplay between TIP60 autoacetylation and SIRT1-mediated deacetylation fine-tunes TIP60 function.

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