Histone deacetylase 4 interacts with 53BP1 to mediate the DNA damage response

J Cell Biol. 2003 Mar 31;160(7):1017-27. doi: 10.1083/jcb.200209065.

Abstract

Anumber of proteins are recruited to nuclear foci upon exposure to double-strand DNA damage, including 53BP1 and Rad51, but the precise role of these DNA damage-induced foci remain unclear. Here we show in a variety of human cell lines that histone deacetylase (HDAC) 4 is recruited to foci with kinetics similar to, and colocalizes with, 53BP1 after exposure to agents causing double-stranded DNA breaks. HDAC4 foci gradually disappeared in repair-proficient cells but persisted in repair-deficient cell lines or cells irradiated with a lethal dose, suggesting that resolution of HDAC4 foci is linked to repair. Silencing of HDAC4 via RNA interference surprisingly also decreased levels of 53BP1 protein, abrogated the DNA damage-induced G2 delay, and radiosensitized HeLa cells. Our combined results suggest that HDAC4 is a critical component of the DNA damage response pathway that acts through 53BP1 and perhaps contributes in maintaining the G2 cell cycle checkpoint.

Publication types

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

MeSH terms

  • Carrier Proteins / metabolism*
  • Cell Line
  • Cell Nucleus / drug effects
  • Cell Nucleus / metabolism
  • Cell Nucleus / radiation effects
  • DNA Damage*
  • DNA Repair
  • DNA-Binding Proteins / genetics
  • DNA-Binding Proteins / metabolism
  • Dose-Response Relationship, Radiation
  • Etoposide / pharmacology
  • G2 Phase
  • Gamma Rays / adverse effects
  • Histone Deacetylases / drug effects
  • Histone Deacetylases / metabolism*
  • Histone Deacetylases / radiation effects
  • Humans
  • Hydroxamic Acids / pharmacology
  • Intracellular Signaling Peptides and Proteins*
  • Kinetics
  • Mutation
  • Nuclear Proteins / genetics
  • Nuclear Proteins / metabolism*
  • Nucleic Acid Synthesis Inhibitors / pharmacology
  • Phosphoproteins*
  • Protein Synthesis Inhibitors / pharmacology
  • RNA, Small Interfering / metabolism
  • Repressor Proteins / drug effects
  • Repressor Proteins / metabolism*
  • Repressor Proteins / radiation effects
  • Tumor Cells, Cultured
  • Tumor Suppressor p53-Binding Protein 1

Substances

  • Carrier Proteins
  • DNA-Binding Proteins
  • Hydroxamic Acids
  • Intracellular Signaling Peptides and Proteins
  • Nuclear Proteins
  • Nucleic Acid Synthesis Inhibitors
  • Phosphoproteins
  • Protein Synthesis Inhibitors
  • RNA, Small Interfering
  • Repressor Proteins
  • TP53BP1 protein, human
  • Tumor Suppressor p53-Binding Protein 1
  • trichostatin A
  • Etoposide
  • HDAC4 protein, human
  • Histone Deacetylases