• Register
X
Forgot Password

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

X

Leaving Community

Are you sure you want to leave this community? Leaving the community will revoke any permissions you have been granted in this community.

No
Yes

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

Authors

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

Journal

Molecular cell

Publication Data

December 9, 2005

Associated Grants

  • Agency: NIAID NIH HHS, Id: AI45587

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