Gene interactions and pathways from curated databases and text-mining
J Biol Chem 2002, PMID: 12063252

Phosphatidylinositol 3-kinase/Akt stimulates androgen pathway through GSK3beta inhibition and nuclear beta-catenin accumulation.

Sharma, Manju; Chuang, William W; Sun, Zijie

PI3K/Akt plays a critical role in prostate cancer cell growth and survival. Recent studies have shown that the effect of PI3K/Akt in prostate cells is mediated through androgen signaling. The PI3K inhibitor, LY294002, and a tumor suppressor, PTEN, negatively regulate the PI3K/Akt pathway and repress AR activity. However, the molecular mechanisms whereby PI3K/Akt and PTEN regulate the androgen pathway are currently unclear. Here, we demonstrate that blocking the PI3K/Akt pathway reduces the expression of an endogenous AR target gene. Moreover, we show that the repression of AR activity by LY294002 is mediated through phosphorylation and inactivation of GSK3beta, a downstream substrate of PI3K/Akt, which results in the nuclear accumulation of beta-catenin. Given the recent evidence that beta-catenin acts as a coactivator of AR, our findings suggest a novel mechanism by which PI3K/Akt modulates androgen signaling. In a PTEN-null prostate cancer cell line, we show that PTEN expression reduces beta-catenin-mediated augmentation of AR transactivation. Using the mutants of beta-catenin, we further demonstrate that the repressive effect of PTEN is mediated by a GSK3beta-regulated degradation of beta-catenin. Our results delineate a novel link among the PI3K, wnt, and androgen pathways and provide fresh insights into the mechanisms of prostate tumor development and progression.

Diseases/Pathways annotated by Medline MESH: Prostatic Neoplasms
Document information provided by NCBI PubMed

Text Mining Data

3-kinase/Akt → beta-catenin: " Phosphatidylinositol 3-kinase/Akt stimulates androgen pathway through GSK3beta inhibition and nuclear beta-catenin accumulation "

Phosphatidylinositol 3-kinase/Akt → beta-catenin: " Phosphatidylinositol 3-kinase/Akt stimulates androgen pathway through GSK3beta inhibition and nuclear beta-catenin accumulation "

beta-catenin → PTEN: " Using the mutants of beta-catenin, we further demonstrate that the repressive effect of PTEN is mediated by a GSK3beta regulated degradation of beta-catenin "

beta-catenin — GSK3beta: " Using the mutants of beta-catenin, we further demonstrate that the repressive effect of PTEN is mediated by a GSK3beta regulated degradation of beta-catenin "

Manually curated Databases

  • OpenBEL Selventa BEL large corpus: AR → CTNNB1 (directlyIncreases, CTNNB1 Activity)
    Evidence: Moreover, we show that the repression of AR activity by LY294002 is mediated through phosphorylation and inactivation of GSK3beta, a downstream substrate of PI3K/Akt, which results in the nuclear accumulation of beta-catenin The activation of Akt results in the phosphorylation of a number of downstream substrates such as glycogen synthase kinase (GSK3) It has been shown that GSK3 plays an important role in the Wnt pathway by regulating the degradation of -catenin Recently, a specific protein-pro...
  • OpenBEL Selventa BEL large corpus: GSK3B → GSK3B (directlyDecreases, GSK3B Activity)
    Evidence: Moreover, we show that the repression of AR activity by LY294002 is mediated through phosphorylation and inactivation of GSK3beta, a downstream substrate of PI3K/Akt, which results in the nuclear accumulation of beta-catenin The activation of Akt results in the phosphorylation of a number of downstream substrates such as glycogen synthase kinase (GSK3) It has been shown that GSK3 plays an important role in the Wnt pathway by regulating the degradation of -catenin Recently, a specific protein-pro...
  • OpenBEL Selventa BEL large corpus: O/5 complex () → PTEN (decreases, PTEN Activity, Activity)
    Evidence: The PI3K inhibitor, LY294002, and a tumor suppressor, PTEN, negatively regulate the PI3K/Akt pathway and repress AR activity.
  • OpenBEL Selventa BEL large corpus: GSK3B → PTEN (increases, PTEN Activity, GSK3B Activity)
    Evidence: Modified assertion