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Sci. Signal., 27 November 2012
[DOI: 10.1126/scisignal.2003223]

Supplementary Materials for:

Regulation of Phosphatidylinositol-5-Phosphate Signaling by Pin1 Determines Sensitivity to Oxidative Stress

Willem-Jan Keune, David R. Jones, Yvette Bultsma, Lilly Sommer, Xiao Zhen Zhou, Kun Ping Lu, Nullin Divecha*

*To whom correspondence should be addressed. E-mail: ndivecha{at}picr.man.ac.uk

This PDF file includes:

  • Fig. S1. Binding of PIPK4β peptides to Pin1 requires the Pin1-WW domain.
  • Fig. S2. Phosphorylation of Thr322 and Ser326 of PIP4Kβ contributes to its interaction with Pin1.
  • Fig. S3. Antibodies recognizing phosphorylated Ser326 peptide show reduced recognition of peptides phosphorylated at both Thr322 and Ser326.
  • Fig. S4. The localization, abundance, and rate of degradation of PIP4Ks are not altered when Pin1 abundance is reduced.
  • Fig. S5. H2O2 treatment increases the abundance of PtdIns5P, which is further increased by knockdown of PIP4Kα and PIP4Kβ.
  • Fig. S6. PIP4Kβ and Pin1 colocalize in the nucleus.
  • Fig. S7. Reexpression of Pin1 in Pin1–/– MEFs reconstitutes sensitivity to H2O2.
  • Fig. S8. Knockout of Pin1 does not alter the kinetics of Akt activation in response to insulin or H2O2.
  • Fig. S9. Overexpression of PIP4Kα in wild-type or Pin1–/– MEFs does not alter their rate of proliferation.
  • Fig. S10. Overexpression of PIP4Kα in wild-type or Pin1–/– MEFs does not alter the expression of p27 or cyclin D1.
  • Table S1. shRNA targeting sequences and qRT-PCR primer sequences.

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Citation: W.-J. Keune, D. R. Jones, Y. Bultsma, L. Sommer, X. Z. Zhou, K. P. Lu, N. Divecha, Regulation of Phosphatidylinositol-5-Phosphate Signaling by Pin1 Determines Sensitivity to Oxidative Stress. Sci. Signal. 5, ra86 (2012).

© 2012 American Association for the Advancement of Science


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