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J. Biol. Chem., Vol. 281, Issue 39, 28575-28583, September 29, 2006

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Binding of p53 to the Central Domain of Mdm2 Is Regulated by Phosphorylation^*

From the Institute of Toxicology and Genetics, Forschungszentrum Karlsruhe, 76021 Karlsruhe, Germany

The Mdm2 protein is the major regulator of the tumor suppressor protein p53. We show that the p53 protein associates both with the N-terminal and with the central domain of Mdm2. The central p53-binding site of Mdm2 encompasses amino acids 235–300. Binding of p53 to the central domain is significantly enhanced after phosphorylation of the central domain of Mdm2. The N-terminal and central domains of Mdm2 act synergistically in binding to p53. p53 mutants that have mutations in the tetramerization domain and that fail to oligomerize do not show such an enhancement of binding in the presence of the other binding site.

Received for publication, December 14, 2005 , and in revised form, July 14, 2006.

^* This work was supported by Deutsche Forschungsgemeinschaft Grant BL151/03. 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: Institute of Toxicology and Genetics, Forschungszentrum Karlsruhe, P.O. Box 3640, 76021 Karlsruhe, Germany. Tel.: 07247-82-2634; Fax: 07247-82-3354; E-mail: christine.blattner{at}itg.fzk.de.

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