B56-containing PP2A dephosphorylate ERK and their activity is controlled by the early gene IEX-1 and ERK.

@article{Letourneux2006B56containingPD,
  title={B56-containing PP2A dephosphorylate ERK and their activity is controlled by the early gene IEX-1 and ERK.},
  author={Claire Letourneux and G{\'e}raldine Rocher and Françoise Porteu},
  journal={The EMBO journal},
  year={2006},
  volume={25 4},
  pages={
          727-38
        }
}
The protein phosphatase 2A (PP2A) acts on several kinases in the extracellular signal-regulated kinase (ERK) signaling pathway but whether a specific holoenzyme dephosphorylates ERK and whether this activity is controlled during mitogenic stimulation is unknown. By using both RNA interference and overexpression of PP2A B regulatory subunits, we show that B56, but not B, family members of PP2A increase ERK dephosphorylation, without affecting its activation by MEK. Induction of the early gene… CONTINUE READING

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