Generation of constitutively active p90 ribosomal S6 kinase in vivo. Implications for the mitogen-activated protein kinase-activated protein kinase family.

@article{PoteetSmith1999GenerationOC,
  title={Generation of constitutively active p90 ribosomal S6 kinase in vivo. Implications for the mitogen-activated protein kinase-activated protein kinase family.},
  author={Celeste E Poteet-Smith and Jeffrey A. Smith and Deborah A. Lannigan and Tiffany A. Freed and Thomas W. Sturgill},
  journal={The Journal of biological chemistry},
  year={1999},
  volume={274 32},
  pages={22135-8}
}
p90 ribosomal S6 kinases (RSKs), containing two distinct kinase catalytic domains, are phosphorylated and activated by extracellular signal-regulated kinase (ERK). The amino-terminal kinase domain (NTD) of RSK phosphorylates exogenous substrates, whereas the carboxyl-terminal kinase domain (CTD) autophosphorylates Ser-386. A conserved putative autoinhibitory alpha helix is present in the carboxyl-terminal tail of the RSK isozymes ((697)HLVKGAMAATYSALNR(712) of RSK2). Here, we demonstrate that… CONTINUE READING

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