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Phosphorylation and Stabilization of TAp63γ by IκB Kinase-β*

Post-translational modification of the p53 family members is key to their regulation. Here we report the phosphorylation of TAp63γ, but not ΔNp63γ, by IκB kinase β (IKKβ). Activation of IKKβ by γ radiation or tumor necrosis factor-α led to increased TAp63γ protein levels in cells. IKKβ, but not its kinase-defective mutant IKKβ-K44A, led to this observed stabilization of TAp63γ. This stabilization of TAp63γ in response to γ radiation was significantly decreased in the absence of IKKβ. Phosphorylation of TAp63γ blocks ubiquitylation and possible degradation of this protein. We postulate that phosphorylation of TAp63γ by IKKβ stabilizes the TAp63γ protein by blocking ubiquitylation-dependent degradation of this protein.