Histone acetyltransferases interact with and acetylate p70 ribosomal S6 kinases in vitro and in vivo.

@article{Fenton2010HistoneAI,
  title={Histone acetyltransferases interact with and acetylate p70 ribosomal S6 kinases in vitro and in vivo.},
  author={Timothy Robert Fenton and Jodie Gwalter and Johan Ericsson and Ivan T Gout},
  journal={The international journal of biochemistry & cell biology},
  year={2010},
  volume={42 2},
  pages={
          359-66
        }
}
The 70kDa ribosomal protein S6 kinases (S6K1 and S6K2) play important roles in the regulation of protein synthesis, cell growth and survival. S6Ks are activated in response to mitogen stimulation and nutrient sufficiency by the phosphorylation of conserved serine and threonine residues. Here we show for the first time, that in addition to phosphorylation, S6Ks are also targeted by lysine acetylation. Following mitogen stimulation, S6Ks interact with the p300 and p300/CBP-associated factor (PCAF… CONTINUE READING

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