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