Binding of P53 to the central domain of MDM2 is regulated by phosphorylation

doi:10.1074/jbc.M513311200

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Papers In Press, published online ahead of print July 26, 2006
J. Biol. Chem, 10.1074/jbc.M513311200
Submitted on December 14, 2005
Revised on July 14, 2006
Accepted on July 26, 2006

Binding of P53 to the central domain of MDM2 is regulated by phosphorylation

Roman Kulikov, Markus Winter, and Christine Blattner

Institute of Toxicology & Genetics, Forschungszentrum Karlsruhe, Karlsruhe 76021

Corresponding Author: christine.blattner{at}itg.fzk.de

The Mdm2 protein is the major regulator of the tumor suppressor protein p53. We show that the p53 protein associates both with the amino terminal and with the central domain of Mdm2. The central p53 binding site of Mdm2 encompasses amino acids 235 to 300. Binding of p53 to the central domain is significantly enhanced after phosphory-lation of the central domain of Mdm2. The amino terminal and central domains of Mdm2 act synergistically in binding to p53. P53 mutants with mutations in the tetramerization domain and which fail to oligomerize do not show such an enhancement in binding in the presence of the other binding site.

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