Phosphorylation of p53 serine 15 increases interaction with CBP

Paul F. Lambert, Fatah Kashanchi, Michael F. Radonovich, Ramin Shiekhattar, John N. Brady

Research output: Contribution to journalArticle

344 Scopus citations

Abstract

p53 exerts its cell cycle regulatory effects through its ability to function as a sequence-specific DNA binding transcription factor. CREB- binding protein (CBP)/p300, through its interaction with the N terminus of p53, acts as a coactivator for p53 and increases the sequence-specific DNA- binding activity of p53 by acetylating its C terminus. The same N-terminal domain of p53 has recently been shown to be phosphorylated at Ser15 in response to γ-irradiation. Remarkably, we now demonstrate that phosphorylation of p53 at Ser15 increases its ability to recruit CBP/p300. The increase in CBP/p300 binding was followed by an increase in the overall level of acetylation of the C terminus of p53. These results provide a mechanism for the activation of p53-regulated genes following DNA damage, through a signaling pathway linking p53 N-terminal kinase and C-terminal acetyltransferase activities.

Original languageEnglish (US)
Pages (from-to)33048-33053
Number of pages6
JournalJournal of Biological Chemistry
Volume273
Issue number49
DOIs
StatePublished - Dec 4 1998

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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