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Akt suppresses androgen-induced apoptosis by phosphorylating and inhibiting androgen receptor.

Whereas several apoptosis-related proteins have been linked to the antiapoptotic effects of Akt serine-threonine kinase, the search continues to explain the Akt signaling role in promoting cell survival via antiapoptotic effects. Here, we demonstrate that Akt phosphorylates the androgen receptor (AR) at Ser-210 and Ser-790. A mutation at AR Ser-210 results in the reversal of Akt-mediated suppression of AR transactivation. Activation of the phosphatidylinositol-3-OH kinase/Akt pathway results in the suppression of AR target genes, such as p21, and the decrease of androgen/AR-mediated apoptosis, which may involve the inhibition of interaction between AR and AR coregulators. Together, these findings provide a molecular basis for cross-talk between two signaling pathways at the level of Akt and AR-AR coregulators that may help us to better understand the roles of Akt in the androgen/AR-mediated apoptosis.

Pubmed ID: 11404460


  • Lin HK
  • Yeh S
  • Kang HY
  • Chang C


Proceedings of the National Academy of Sciences of the United States of America

Publication Data

June 19, 2001

Associated Grants


Mesh Terms

  • Amino Acid Substitution
  • Androgen Receptor Antagonists
  • Apoptosis
  • Chromones
  • Dihydrotestosterone
  • Enzyme Inhibitors
  • Gene Expression Regulation, Neoplastic
  • Humans
  • Male
  • Morpholines
  • Mutagenesis, Site-Directed
  • Phosphatidylinositol 3-Kinases
  • Phosphorylation
  • Prostatic Neoplasms
  • Protein-Serine-Threonine Kinases
  • Proto-Oncogene Proteins
  • Proto-Oncogene Proteins c-akt
  • Receptors, Androgen
  • Recombinant Proteins
  • Serine
  • Signal Transduction
  • Transcriptional Activation
  • Transfection
  • Tumor Cells, Cultured