PTEN Protein Phosphatase Activity Correlates with Control of Gene Expression and Invasion, a Tumor-Suppressing Phenotype, But Not with AKT Activity

Priyanka Tibarewal, Georgios Zilidis, Laura Spinelli, Nick Schurch, Helene Maccario, Alexander Gray, Nevin M. Perera, Lindsay Davidson, Geoffrey J. Barton, Nick R. Leslie*

*To whom correspondence should be addressed. E-mail: n.r.leslie{at}dundee.ac.uk

This PDF file includes:

• Materials and Methods
• Fig. S1. Regulation of AKT phosphorylation by wild-type PTEN and PTEN Y138L.
• Fig. S2. Assigned gene sets associated with transcript changes induced by wild-type PTEN expression in U87MG cells.
• Fig. S3. Autodephosphorylation analysis of PTEN mutant proteins.
• Fig. S4. Effects of kinase inhibition and hyperosmotic stress on PTEN Thr³⁶⁶ phosphorylation.
• Fig. S5. Further analysis of PTEN Thr³⁶⁶ phosphorylation.
• Fig. S6. Effects of PTEN on U87MG cell morphology in 3D Matrigel cultures.
• Fig. S7. Quantitation of blotting data.
• Fig. S8. Quantitation and statistical analysis of blotting data.
• Table S1. Wild-type PTEN–responsive gene list used for clinical data comparison.
  
• References

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© 2012 American Association for the Advancement of Science