The Tumor Suppressor PTEN Is Phosphorylated by the Protein Kinase CK2 at Its C Terminus

By Josema Torres, R. Pulido. Journal of Biological Chemistry, 2001

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The tumor suppressor phosphatase PTEN regulates cell migration, growth, and survival by dephosphorylating phosphatidylinositol second messengers and signaling phosphoproteins. PTEN possesses a C-terminal noncatalytic regulatory domain that contains multiple putative phosphorylation sites, which could play an important role in the control of its biological activity. The protein kinase CK2 phosphorylated, in a constitutive manner, a cluster of Ser/Thr residues located at the PTEN C terminus. PTEN-phosphorylated defective mutants showed decreased stability in comparison with wild type PTEN and were more rapidly degraded by the proteasome. Inhibition of PTEN phosphorylation by the CK2 inhibitor 5,6-dichloro-1-β-d-ribofuranosyl-benzimidazole also diminished the PTEN protein content. Our results support the notion that proper phosphorylation of PTEN by CK2 is important for PTEN protein stability to proteasome-mediated degradation.

Subfields: Genetics, Immunology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/7d875104c0d0daf8cbf4ea420d3a1fb7c3d22343

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In Genetics

  1. P. Pandolfi
  2. Arkaitz Carracedo
  3. David M. Sabatini

In Immunology

  1. P. Pandolfi
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In Molecular Biology

  1. P. Pandolfi
  2. Arkaitz Carracedo
  3. Paul Tempst
  4. H. Erdjument‐Bromage
  5. L. Salmena
  6. Xuejun Jiang
  7. A. Alimonti
  8. David M. Sabatini

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