Phosphoinositide (3,4,5)-triphosphate binding to phosphoinositide-dependent kinase 1 regulates a protein kinase B/Akt signaling threshold that dictates T-cell migration, not proliferation.

@article{Waugh2009PhosphoinositideB,
  title={Phosphoinositide (3,4,5)-triphosphate binding to phosphoinositide-dependent kinase 1 regulates a protein kinase B/Akt signaling threshold that dictates T-cell migration, not proliferation.},
  author={Caryll M. Waugh and Linda V Sinclair and David K Finlay and Jos{\'e} Ram{\'o}n Bayascas and Doreen A Cantrell},
  journal={Molecular and cellular biology},
  year={2009},
  volume={29 21},
  pages={5952-62}
}
The present study explored the consequences of phosphoinositide (3,4,5)-triphosphate [PI(3,4,5)P(3)] binding to the pleckstrin homology (PH) domain of the serine/threonine kinase 3-phosphoinositide-dependent kinase 1 (PDK1). The salient finding is that PDK1 directly transduces the PI(3,4,5)P(3) signaling that determines T-cell trafficking programs but not T-cell growth and proliferation. The integrity of the PDK1 PH domain thus is not required for PDK1 catalytic activity or to support cell… CONTINUE READING

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The kinase PDK1 integrates T cell antigen receptor and CD28 coreceptor signaling to induce NF-.B and activate T cells

  • S. G. Park, J. Schulze-Luehrman, +4 authors S. Ghosh
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