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}mcgill.ca

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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Other Supplementary Material for this manuscript includes the following:

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

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