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