PTEN modulates cell cycle progression and cell survival by regulating phosphatidylinositol 3,4,5,-trisphosphate and Akt/protein kinase B signaling pathway

Proc Natl Acad Sci U S A. 1999 May 25;96(11):6199-204. doi: 10.1073/pnas.96.11.6199.

Abstract

To investigate the molecular basis of PTEN-mediated tumor suppression, we introduced a null mutation into the mouse Pten gene by homologous recombination in embryonic stem (ES) cells. Pten-/- ES cells exhibited an increased growth rate and proliferated even in the absence of serum. ES cells lacking PTEN function also displayed advanced entry into S phase. This accelerated G1/S transition was accompanied by down-regulation of p27(KIP1), a major inhibitor for G1 cyclin-dependent kinases. Inactivation of PTEN in ES cells and in embryonic fibroblasts resulted in elevated levels of phosphatidylinositol 3,4,5,-trisphosphate, a product of phosphatidylinositol 3 kinase. Consequently, PTEN deficiency led to dosage-dependent increases in phosphorylation and activation of Akt/protein kinase B, a well-characterized target of the phosphatidylinositol 3 kinase signaling pathway. Akt activation increased Bad phosphorylation and promoted Pten-/- cell survival. Our studies suggest that PTEN regulates the phosphatidylinositol 3,4, 5,-trisphosphate and Akt signaling pathway and consequently modulates two critical cellular processes: cell cycle progression and cell survival.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Cell Cycle / physiology*
  • Cell Cycle Proteins*
  • Cell Division
  • Cell Survival
  • Cells, Cultured
  • Cyclin-Dependent Kinase Inhibitor p27
  • Embryo, Mammalian
  • Genes, Tumor Suppressor*
  • Genomic Library
  • In Situ Nick-End Labeling
  • Kinetics
  • Mice
  • Mice, Knockout
  • Microtubule-Associated Proteins / genetics
  • Microtubule-Associated Proteins / metabolism
  • PTEN Phosphohydrolase
  • Phosphatidylinositol Phosphates / metabolism*
  • Phosphoric Monoester Hydrolases / deficiency
  • Phosphoric Monoester Hydrolases / genetics*
  • Phosphoric Monoester Hydrolases / physiology
  • Protein Serine-Threonine Kinases*
  • Proto-Oncogene Proteins / metabolism*
  • Proto-Oncogene Proteins c-akt
  • Recombination, Genetic
  • Restriction Mapping
  • Signal Transduction
  • Stem Cells / cytology
  • Tumor Suppressor Proteins*

Substances

  • Cdkn1b protein, mouse
  • Cell Cycle Proteins
  • Microtubule-Associated Proteins
  • Phosphatidylinositol Phosphates
  • Proto-Oncogene Proteins
  • Tumor Suppressor Proteins
  • phosphatidylinositol 3,4,5-triphosphate
  • Cyclin-Dependent Kinase Inhibitor p27
  • Protein Serine-Threonine Kinases
  • Proto-Oncogene Proteins c-akt
  • Phosphoric Monoester Hydrolases
  • PTEN Phosphohydrolase