Phosphorylation of the PTEN tail acts as an inhibitory switch by preventing its recruitment into a protein complex.

@article{Vazquez2001PhosphorylationOT,
  title={Phosphorylation of the PTEN tail acts as an inhibitory switch by preventing its recruitment into a protein complex.},
  author={Francisca Vazquez and Steven R. Grossman and Yoshinori Takahashi and Mihail Rokas and Nobuhiro Nakamura and William R Sellers},
  journal={The Journal of biological chemistry},
  year={2001},
  volume={276 52},
  pages={48627-30}
}
PTEN is a tumor suppressor protein that functions, in large part, by dephosphorylating the lipid second messenger phosphatidylinositol 3,4,5-trisphosphate and by doing so antagonizing the action of phosphoinositide 3-kinase. PTEN structural domains include an N-terminal phosphatase domain, a lipid-binding C2 domain, and a 50-amino acid C-terminal tail that contains a PDZ binding sequence. We showed previously that phosphorylation of the PTEN tail negatively regulates PTEN activity. We now show… CONTINUE READING

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