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J. Biol. Chem., Vol. 280, Issue 29, 27443-27448, July 22, 2005

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The Chaperone-associated Ubiquitin Ligase CHIP Is Able to Target p53 for Proteasomal Degradation^*

Claudia Esser, Martin Scheffner, and Jörg Höhfeld¶

From the Institute for Cell Biology and Bonner Forum Biomedizin, Rheinische Friedrich-Wilhelms-University Bonn, Ulrich-Haberland-Str. 61a, D-53121 Bonn, Germany and the Department of Biology, Laboratory for Biochemistry, University of Konstanz, 78457 Konstanz, Germany

The cellular level of the tumor suppressor p53 is tightly regulated through induced degradation via the ubiquitin/proteasome system. The ubiquitin ligase Mdm2 plays a pivotal role in stimulating p53 turnover. However, recently additional ubiquitin ligases have been identified that participate in the degradation of the tumor suppressor. Apparently, multiple degradation pathways are employed to ensure proper destruction of p53. Here we show that the chaperone-associated ubiquitin ligase CHIP is able to induce the proteasomal degradation of p53. CHIP-induced degradation was observed for mutant p53, which was previously shown to associate with the chaperones Hsc70 and Hsp90, and for the wild-type form of the tumor suppressor. Our data reveal that mutant and wild-type p53 transiently associate with molecular chaperones and can be diverted onto a degradation pathway through this association.

Received for publication, February 10, 2005 , and in revised form, May 13, 2005.

^* 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.

^¶ To whom correspondence should be addressed. Tel.: 49-228-735308; Fax: 49-228-735302; E-mail: hoehfeld{at}uni-bonn.de.

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