Figure 1 | Scientific Reports

Figure 1

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

Figure 1

Auto inhibition is more predominant for the third phosphorylation site. (a) Phosphorylation kinetics on S585 in the p63 PAD peptide with the CK1δ kinase domain alone (black), full length kinase (red) and prephosphorylated full length kinase (blue) measured by mass spectrometry. The panels shown in (b–d) represent the phosphorylation kinetics on S588, S591 and T594 respectively. While the kinetics of S585 and S588 is slowed down, the phosphorylation of S591 and the subsequent T594 is almost completely inhibited by auto-phosphorylation in the C-terminus of full length kinase. (e) Sequence of the p63 PAD peptide. The CHK2 site is labeled orange, the four CK1 sites are marked red. Data points represent the average and standard deviation obtained from three individual experiments.

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