RSK1 drives p27Kip1 phosphorylation at T198 to promote RhoA inhibition and increase cell motility.

@article{Larrea2009RSK1DP,
  title={RSK1 drives p27Kip1 phosphorylation at T198 to promote RhoA inhibition and increase cell motility.},
  author={Michelle D Larrea and Feng Hong and Seth A. Wander and Thiago G da Silva and D. M. Helfman and Deborah A. Lannigan and Jeffrey A. Smith and Joyce M Slingerland},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2009},
  volume={106 23},
  pages={9268-73}
}
p90 ribosomal S6 kinase (RSK1) is an effector of both Ras/MEK/MAPK and PI3K/PDK1 pathways. We present evidence that RSK1 drives p27 phosphorylation at T198 to increase RhoA-p27 binding and cell motility. RSK1 activation and p27pT198 both increase in early G(1). As for many kinase-substrate pairs, cellular RSK1 coprecipitates with p27. siRNA to RSK1 and RSK1… CONTINUE READING