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Sci. Signal., 22 December 2009
[DOI: 10.1126/scisignal.2000389]

Supplementary Materials for:

Tumor Suppression by PTEN Requires the Activation of the PKR-eIF2α Phosphorylation Pathway

Zineb Mounir, Jothi Latha Krishnamoorthy, Gavin P. Robertson, Donalyn Scheuner, Randal J. Kaufman, Maria-Magdalena Georgescu, Antonis E. Koromilas*

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

This PDF file includes:

  • Fig. S1. Effect of doxycycline on the phosphorylation of eIF2α in parental U87 and U251 cells.
  • Fig. S2. Phosphatase-deficient mutants of PTEN do not affect the phosphorylation of S6 or 4EBP-1.
  • Fig. S3. The kinases PERK and GCN2 are not activated by PTEN.
  • Fig. S4. Detection of the activation of PKR by PTEN in vivo.
  • Fig. S5. Role of PKR in PTEN-mediated inhibition of PC-3 cell proliferation.
  • Fig. S6. Role of phosphorylated eIF2α in PTEN-mediated inhibition of PC-3 cell proliferation.
  • Fig. S7. Lack of a physical interaction between PKR and PTEN.
  • Fig. S8. The PKR-eIF2α phosphorylation pathway acts downstream of PTEN.

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Citation: Z. Mounir, J. L. Krishnamoorthy, G. P. Robertson, D. Scheuner, R. J. Kaufman, M.-M. Georgescu, A. E. Koromilas, Tumor Suppression by PTEN Requires the Activation of the PKR-eIF2α Phosphorylation Pathway. Sci. Signal. 2, ra85 (2009).

© 2009 American Association for the Advancement of Science


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