SIRT1 regulates autoacetylation and histone acetyltransferase activity of TIP60

Jiadong Wang, Junjie Chen

Research output: Contribution to journalArticle

69 Citations (Scopus)

Abstract

The histone acetyltransferase TIP60, a frequent target of monoallelic loss in human carcinomas, can acetylate many substrates, including histones and p53, and thus promote apoptosis following UV radiation. Here we showed that TIP60 is autoacetylated in response to UV damage, which is critically important for TIP60 activation. Mechanistically we demonstrated that TIP60 autoacetylation leads to the dissociation of TIP60 oligomer and enhances its interaction with substrates. Moreover, we identified SIRT1 that specifically deacetylates TIP60 and negatively regulates TIP60 activity in vivo. Taken together, our data reveal TIP60 autoacetylation as a key step in the control of its histone acetyltransferase activity and function in response to DNA damage.

Original languageEnglish (US)
Pages (from-to)11458-11464
Number of pages7
JournalJournal of Biological Chemistry
Volume285
Issue number15
DOIs
StatePublished - Apr 9 2010

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Histone Acetyltransferases
Substrates
Oligomers
Ultraviolet radiation
Histones
DNA Damage
Chemical activation
Radiation
Apoptosis
Carcinoma
DNA

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

SIRT1 regulates autoacetylation and histone acetyltransferase activity of TIP60. / Wang, Jiadong; Chen, Junjie.

In: Journal of Biological Chemistry, Vol. 285, No. 15, 09.04.2010, p. 11458-11464.

Research output: Contribution to journalArticle

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