Preparing your results

Our searching services are busy right now. Your search will reload in five seconds.

Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.

gamma-H2AX dephosphorylation by protein phosphatase 2A facilitates DNA double-strand break repair.

Phosphorylated histone H2AX (gamma-H2AX) forms foci over large chromatin domains surrounding double-stranded DNA breaks (DSB). These foci recruit DSB repair proteins and dissolve during or after repair is completed. How gamma-H2AX is removed from chromatin remains unknown. Here, we show that protein phosphatase 2A (PP2A) is involved in removing gamma-H2AX foci. The PP2A catalytic subunit [PP2A(C)] and gamma-H2AX coimmunoprecipitate and colocalize in DNA damage foci and PP2A dephosphorylates gamma-H2AX in vitro. The recruitment of PP2A(C) to DNA damage foci is H2AX dependent. When PP2A(C) is inhibited or silenced by RNA interference, gamma-H2AX foci persist, DNA repair is inefficient, and cells are hypersensitive to DNA damage. The effect of PP2A on gamma-H2AX levels is independent of ATM, ATR, or DNA-PK activity.

Pubmed ID: 16310392


  • Chowdhury D
  • Keogh MC
  • Ishii H
  • Peterson CL
  • Buratowski S
  • Lieberman J


Molecular cell

Publication Data

December 9, 2005

Associated Grants

  • Agency: NIAID NIH HHS, Id: AI45587
  • Agency: NIGMS NIH HHS, Id: R01 GM054096

Mesh Terms

  • Animals
  • Ataxia Telangiectasia Mutated Proteins
  • Cell Cycle Proteins
  • Cell Line
  • DNA Damage
  • DNA Repair
  • DNA-Activated Protein Kinase
  • DNA-Binding Proteins
  • Fibroblasts
  • HeLa Cells
  • Histones
  • Humans
  • In Vitro Techniques
  • Mice
  • Phosphoprotein Phosphatases
  • Phosphorylation
  • Protein Phosphatase 2
  • Protein-Serine-Threonine Kinases
  • Tumor Suppressor Proteins