A role for ATR in the DNA damage-induced phosphorylation of p53

Genes Dev. 1999 Jan 15;13(2):152-7. doi: 10.1101/gad.13.2.152.

Abstract

Phosphorylation at Ser-15 may be a critical event in the up-regulation and functional activation of p53 during cellular stress. In this report we provide evidence that the ATM-Rad3-related protein ATR regulates phosphorylation of Ser-15 in DNA-damaged cells. Overexpression of catalytically inactive ATR (ATRki) in human fibroblasts inhibited Ser-15 phosphorylation in response to gamma-irradiation and UV light. In gamma-irradiated cells, ATRki expression selectively interfered with late-phase Ser-15 phosphorylation, whereas ATRki blocked UV-induced Ser-15 phosphorylation in a time-independent manner. ATR phosphorylated p53 at Ser-15 and Ser-37 in vitro, suggesting that p53 is a target for phosphorylation by ATR in DNA-damaged cells.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Ataxia Telangiectasia Mutated Proteins
  • Cell Cycle Proteins / genetics
  • Cell Cycle Proteins / metabolism*
  • DNA Damage / physiology*
  • DNA Damage / radiation effects
  • DNA-Binding Proteins
  • Doxycycline / pharmacology
  • Fibroblasts
  • Gamma Rays
  • Humans
  • K562 Cells
  • Mutation
  • Phosphorylation / drug effects
  • Phosphorylation / radiation effects
  • Precipitin Tests
  • Protein Serine-Threonine Kinases*
  • Proteins / metabolism
  • Recombinant Fusion Proteins / biosynthesis
  • Recombinant Fusion Proteins / immunology
  • Recombinant Fusion Proteins / metabolism
  • Serine / metabolism
  • Time Factors
  • Transfection
  • Tumor Cells, Cultured
  • Tumor Suppressor Protein p53 / metabolism*
  • Tumor Suppressor Proteins
  • Ultraviolet Rays

Substances

  • Cell Cycle Proteins
  • DNA-Binding Proteins
  • Proteins
  • Recombinant Fusion Proteins
  • Tumor Suppressor Protein p53
  • Tumor Suppressor Proteins
  • Serine
  • ATM protein, human
  • ATR protein, human
  • Ataxia Telangiectasia Mutated Proteins
  • Protein Serine-Threonine Kinases
  • Doxycycline