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p70S6 kinase signals cell survival as well as growth, inactivating the pro-apoptotic molecule BAD.

Cytokines often deliver simultaneous, yet distinct, cell growth and cell survival signals. The 70-kDa ribosomal protein S6 kinase (p70S6K) is known to regulate cell growth by inducing protein synthesis components. We purified membrane-based p70S6K as a kinase responsible for site-specific phosphorylation of BAD, which inactivates this proapoptotic molecule. Rapamycin inhibited mitochondrial-based p70S6K, which prevented phosphorylation of Ser-136 on BAD and blocked cell survival induced by insulin-like growth factor 1 (IGF-1). Moreover, IGF-1-induced phosphorylation of BAD Ser-136 was abolished in p70S6K-deficient cells. Thus, p70S6K is itself a dual pathway kinase, signaling cell survival as well as growth through differential substrates which include mitochondrial BAD and the ribosomal subunit S6, respectively.

Pubmed ID: 11493700


  • Harada H
  • Andersen JS
  • Mann M
  • Terada N
  • Korsmeyer SJ


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

Publication Data

August 14, 2001

Associated Grants

  • Agency: NCI NIH HHS, Id: CA50239-13

Mesh Terms

  • Animals
  • Apoptosis
  • Carrier Proteins
  • Cell Division
  • Cell Line
  • Cell Survival
  • Enzyme Inhibitors
  • Insulin-Like Growth Factor I
  • Interleukin-3
  • Mitochondria
  • Models, Biological
  • Phosphorylation
  • Point Mutation
  • Protein Processing, Post-Translational
  • Rats
  • Recombinant Fusion Proteins
  • Ribosomal Protein S6 Kinases
  • Sirolimus
  • bcl-Associated Death Protein