De-RSKing ERK - regulation of ERK1/2-RSK dissociation by phosphorylation within a disordered motif.

@article{Kidger2018DeRSKingE,
  title={De-RSKing ERK - regulation of ERK1/2-RSK dissociation by phosphorylation within a disordered motif.},
  author={Andrew M. Kidger and Simon J Cook},
  journal={The FEBS journal},
  year={2018},
  volume={285 1},
  pages={42-45}
}
The protein kinases ERK1/2 and RSK associate in unstimulated cells but must separate to target other substrates. In this issue, Gógl et al. show that phosphorylation of RSK by active ERK1/2 culminates in the formation of an intramolecular charge clamp between Lys729 and the phosphate group on Ser732. This promotes the dissociation of ERK1/2 from RSK… CONTINUE READING