A phosphatase-independent gain-of-function mutation in PTEN triggers aberrant cell growth in astrocytes through an autocrine IGF-1 loop

Oncogene. 2014 Aug 7;33(32):4114-22. doi: 10.1038/onc.2013.376. Epub 2013 Sep 23.

Abstract

Loss-of-function mutations in the phosphatase PTEN (phosphatase and tensin homolog deleted on chromosome10) contribute to aberrant cell growth in part through upregulation of the mitogenic IGF-1/PI3K/Akt pathway. In turn, this pathway exerts a homeostatic feedback over PTEN. Using mutagenesis analysis to explore a possible impact of this mutual control on astrocyte growth, we found that truncation of the C-terminal region of PTEN (Δ51) associates with a marked increase in NFκB activity, a transcription factor overactivated in astrocyte tumors. Whereas mutations of PTEN are considered to lead to a loss-of-function, PTENΔ51, a truncation that comprises a region frequently mutated in human gliomas, displayed a neomorphic (gain-of-function) activity that was independent of its phosphatase activity. This gain-of-function of PTENΔ51 includes stimulation of IGF-1 synthesis through protein kinase A activation of the IGF-1 promoter. Increased IGF-1 originates an autocrine loop that activates Akt and NFκB. Constitutive activation of NFκB in PTENΔ51-expressing astrocytes leads to aberrant cell growth; astrocytes expressing this mutant PTEN generate colonies in vitro and tumors in vivo. Mutations converting a tumor suppressor such as PTEN into a tumor promoter through a gain-of-function involving IGF-1 production may further our understanding of the role played by this growth factor in glioma growth and help us define druggable targets for personalized therapy.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Astrocytes / cytology*
  • Cell Line, Tumor
  • Cell Proliferation
  • Cyclic AMP-Dependent Protein Kinases / metabolism
  • Gene Expression Regulation, Neoplastic*
  • Glioma / metabolism
  • Humans
  • Insulin-Like Growth Factor I / metabolism*
  • Mice
  • Mice, SCID
  • Mutation*
  • NF-kappa B / metabolism
  • Neoplasm Transplantation
  • PTEN Phosphohydrolase / genetics*
  • PTEN Phosphohydrolase / physiology*
  • Protein Structure, Tertiary
  • Reactive Oxygen Species / metabolism

Substances

  • NF-kappa B
  • Reactive Oxygen Species
  • Insulin-Like Growth Factor I
  • Cyclic AMP-Dependent Protein Kinases
  • PTEN Phosphohydrolase
  • PTEN protein, human