Supplementary Materials

Supplementary Materials for:

Global assessment of its network dynamics reveals that the kinase Plk1 inhibits the phosphatase PP6 to promote Aurora A activity

Arminja N. Kettenbach,* Kate A. Schlosser, Scott P. Lyons, Isha Nasa, Jiang Gui, Mark E. Adamo, Scott A. Gerber*

*Corresponding author. Email: arminja.n.kettenbach{at}dartmouth.edu (A.N.K.); scott.a.gerber{at}dartmouth.edu (S.A.G.)

This PDF file includes:

  • Fig. S1. SDS-PAGE gels of control and Plk1 IPs.
  • Fig. S2. Comparison of the effects of flavopiridol and staurosporine on Plk1 interactions.
  • Fig. S3. GO analyses.
  • Fig. S4. Protein complexes in the Plk1 interactome.
  • Fig. S5. First-degree neighbors of CDK1-targeted Plk1 interactors.
  • Fig. S6. Regulatory subunit interactors of PP6 and Plk1.
  • Fig. S7. Conservation of candidate PBD-binding motifs in PP6R2.
  • Fig. S8. Termination of the Plk1-PP6 interaction.
  • Fig. S9. Dependence of PP1c on Plk1 activity in dephosphorylating the Aurora Aâ€"TPX2 complex.
  • Legends for tables S1 to S5

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Other Supplementary Material for this manuscript includes the following:

  • Table S1 (Microsoft Excel format). SILAC-based identification of kinase inhibitor–responsive Plk1 protein-protein interactions.
  • Table S2 (Microsoft Excel format). Number of SP/TP and SSP/STP motifs in Plk1 interactors.
  • Table S3 (Microsoft Excel format). Wild-type and Pincer mutant Plk1 protein-protein interactions.
  • Table S4 (Microsoft Excel format). SILAC-based identification of Plk1 inhibitor–responsive phosphorylation sites on PP6R2.
  • Table S5 (Microsoft Excel format). In vitro confirmation of CDK1–cyclin B phosphorylation occupancy of PP6R2.

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