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Sci. Signal., 27 September 2011
[DOI: 10.1126/scisignal.2001630]

Supplementary Materials for:

Akt Determines Cell Fate Through Inhibition of the PERK-eIF2α Phosphorylation Pathway

Zineb Mounir, Jothi Latha Krishnamoorthy, Shuo Wang, Barbara Papadopoulou, Shirley Campbell, William J. Muller, Maria Hatzoglou, Antonis E. Koromilas*

*To whom correspondence should be addressed. E-mail: antonis.koromilas{at}

This PDF file includes:

  • Materials and Methods
  • Fig. S1. Specificity of induction of eIF2αP by PI3K inhibitors.
  • Fig. S2. Induction of eIF2α phosphorylation by PI3K inhibition in Drosophila cells.
  • Fig. S3. PKR and HRI are not involved in the induction of eIF2α phosphorylation by PI3K inhibition.
  • Fig. S4. PI3K inhibition does not result in induction of ER stress.
  • Fig. S5. Akt inactivation results in the induction of eIF2α phosphorylation.
  • Fig. S6. PERK is phosphorylated by Akt in vitro.
  • Fig. S7. Akt diminishes the induction of eIF2α phosphorylation in response to oxidative or ER stress in human cells.
  • Fig. S8. Induction of PERK activation and eIF2α phosphorylation by PI3K or Akt inactivation promotes cell survival.
  • Fig. S9. Inactivation of PERK increases the efficacy of tumor treatment with PI3K and Akt inhibitors.
  • Fig. S10. Model of the inhibition of the PERK-eIF2αP arm by Akt.
  • References

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Technical Details

Format: Adobe Acrobat PDF

Size: 743 KB

Other Supplementary Material for this manuscript includes the following:

  • Table S1 (Microsoft Excel format). Results of statistical analysis.

Technical Details

Format: Microsoft Excel

Size: 38 KB

Citation: Z. Mounir, J. L. Krishnamoorthy, S. Wang, B. Papadopoulou, S. Campbell, W. J. Muller, M. Hatzoglou, A. E. Koromilas, Akt Determines Cell Fate Through Inhibition of the PERK-eIF2α Phosphorylation Pathway. Sci. Signal. 4, ra62 (2011).

© 2011 American Association for the Advancement of Science

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