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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