Molecular mechanism for the regulation of protein kinase B/Akt by hydrophobic motif phosphorylation.

@article{Yang2002MolecularMF,
  title={Molecular mechanism for the regulation of protein kinase B/Akt by hydrophobic motif phosphorylation.},
  author={Jing Yang and Peter D. Cron and Vivienne Thompson and Valerie M. Good and Daniel Hess and Brian A. Hemmings and David Barford},
  journal={Molecular cell},
  year={2002},
  volume={9 6},
  pages={1227-40}
}
Protein kinase B/Akt plays crucial roles in promoting cell survival and mediating insulin responses. The enzyme is stimulated by phosphorylation at two regulatory sites: Thr 309 of the activation segment and Ser 474 of the hydrophobic motif, a conserved feature of many AGC kinases. Analysis of the crystal structures of the unphosphorylated and Thr 309 phosphorylated states of the PKB kinase domain provides a molecular explanation for regulation by Ser 474 phosphorylation. Activation by Ser 474… CONTINUE READING
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15 , 6541 – 6551 . receptor

  • D. R. Alessi, S. R. James, +5 authors D. J. Owen
  • Nature
  • 1996
Highly Influential
5 Excerpts

19 , 5061 – 5072

  • A. Balendran, A. Casamayor, +5 authors D. R. Alessi
  • Acta Crystallogr . A
  • 1999
Highly Influential
1 Excerpt

Ten years of protein kinase mutant derivatives were transferred from the pFastBacHTA plasmid B signalling : a hard Akt to follow

  • B. A. Hemmings
  • Biochemistry
  • 2001
1 Excerpt

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