Figure 4 | Scientific Reports

Figure 4

From: Fuzzy interactions between the auto-phosphorylated C-terminus and the kinase domain of CK1δ inhibits activation of TAp63α

Figure 4

Comparison of the phosphorylation kinetics of a wild type p63 PAD peptide (except for the mentioned T586A mutation, shown in blue) with a mutated p63 PAD peptide (shown in yellow) measured with full length CK1δ. Mutating V587 and V589 of p63 PAD to asparagine as a small and polar but not phosphorylatable residue reduces the phosphorylation kinetics of S585 (a). The phosphorylation of S588 is even severely inhibited (b) and the phosphorylation of (c) S591 and (d) T594 can no longer be detected. Experiments with the V587N, V589N mutated PAD peptide were measured in triplicate, the data with the wild type PAD peptide in duplicate. The data shown represent one replicate.

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