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J. Biol. Chem., Vol. 283, Issue 23, 15754-15761, June 6, 2008

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Phosphorylation and Stabilization of TAp63 by IB Kinase-β^*

Mary MacPartlin, Shelya X. Zeng, and Hua Lu¹

From the Center for Hematologic Malignancies, Oregon Health & Science University Cancer Institute, Oregon Health and Science University, Portland, Oregon 97239-3098 and the Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, Indiana 46202

Post-translational modification of the p53 family members is key to their regulation. Here we report the phosphorylation of TAp63, but not Np63, by IB kinase β (IKKβ). Activation of IKKβ by radiation or tumor necrosis factor- led to increased TAp63 protein levels in cells. IKKβ, but not its kinase-defective mutant IKKβ-K44A, led to this observed stabilization of TAp63. This stabilization of TAp63 in response to radiation was significantly decreased in the absence of IKKβ. Phosphorylation of TAp63 blocks ubiquitylation and possible degradation of this protein. We postulate that phosphorylation of TAp63 by IKKβ stabilizes the TAp63 protein by blocking ubiquitylation-dependent degradation of this protein.

Received for publication, February 21, 2008 , and in revised form, April 8, 2008.

^* This work was supported, in whole or in part, by National Institutes of Health Grants CA127724, CA 93614, CA 095441, and CA 079721 (to H. L.) from NCI. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ To whom correspondence should be addressed: Dept. of Biochemistry and Molecular Biology, Indiana University School of Medicine, 635 Barnhill Dr., MS4053, Indianapolis, IN 46202. Tel.: 317-278-0920; Fax: 317-274-4686; E-mail: hualu{at}iupui.edu.

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