Supplementary Materials

This PDF file includes:

  • Fig. S1. Chemical routes for Cys redox modifications in proteins and their detection with commercial reagents.
  • Fig. S2. Analysis of Aurora A purified in the presence of DTT.
  • Fig. S3. Biochemical analysis of Aurora A oxidation.
  • Fig. S4. Analysis of Aurora A and a redox-resistant C290A mutant.
  • Fig. S5. Analysis of C290S and C290D mutants.
  • Fig. S6. Both WT and C290A Aurora A bind to TPX2.
  • Fig. S7. Reversible glutathionylation of Aurora A and AKT.
  • Fig. S8. Taxonomic analysis of conserved Cys residues within the activation segment of all ePKs.
  • Fig. S9. Biochemical analysis of Cys-containing protein kinases.
  • Fig. S10. Thermal profiling and immunoblotting-based redox analysis of Aurora A “DFG +2” kinase mutants.
  • Fig. S11. Kinases having a “T-loop +2” Cys residue that are insensitive to redox-dependent regulation.
  • Fig. S12. Real-time redox analysis of model Tyr kinases and Cys mutants.
  • Fig. S13. Structural models of disulfide-based mechanisms involving activation segment Cys in Ser/Thr kinases.
  • Table S1. Human kinases containing an Aurora A Cys290 equivalent in the activation segment.
  • Table S2. Positional distribution in all human kinases that contain Cys residues in the activation segment.
  • Table S3. Protein kinase enzymes and substrates.
  • Table S4. Yeast strains described in this study.
  • References (146, 147)

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