A Peptide-Based Target Screen Implicates the Protein Kinase CK2 in the Global Regulation of Caspase Signaling

James S. Duncan, Jacob P. Turowec, Kelly E. Duncan, Greg Vilk, Chenggang Wu, Bernhard Lüscher, Shawn S.-C. Li, Greg B. Gloor, David W. Litchfield*

*To whom correspondence should be addressed. E-mail: litchfi{at}uwo.ca

This PDF file includes:

• Methods
• Fig. S1. Phosphorylation of the P2 or P1′ residue prevents cleavage by caspases.
• Fig. S2. Phosphorylation of procaspase-3 by CK2 results in its protection from caspase-mediated cleavage.
• Fig. S3. Mass spectrometric determination of the phosphorylation site of caspase-3.
• Fig. S4. Phosphorylation of procaspase-3 at Thr¹⁷⁴ and Ser¹⁷⁶ protects it from caspase-mediated cleavage.
• Table S3. Proteins identified in the peptide match search that have overlapping CK2 and caspase recognition motifs that are cleaved by caspases in cells.
• Table S4. Proteins identified from the peptide match screen that have overlapping CK2 and caspase recognition motifs and were previously identified to be phosphorylated in cells.
• Table S6. Identification of candidate CK2 and caspase peptide sequences that are sensitive to cleavage by caspases.
  

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Other Supplementary Material for this manuscript includes the following:

• Table S1 (Microsoft Excel format). List of candidate targets of kinases and caspase-3.
• Table S2 (Microsoft Excel format). List of putative targets of CK2 and caspases.
• Table S5 (Microsoft Excel format). Candidate targets of CK2 and caspases that were phosphorylated by GST-CK2α.

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© 2011 American Association for the Advancement of Science