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Molecular and Cellular Biology, May 1999, p. 3257-3266, Vol. 19, No. 5
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

MDM2 Suppresses p73 Function without Promoting p73 Degradation

Xiaoya Zeng,1 Lihong Chen,2 Christine A. Jost,3 Ruth Maya,4 David Keller,1 Xinjiang Wang,4 William G. Kaelin Jr.,3,5 Moshe Oren,4 Jiandong Chen,2 and Hua Lu1,*

Department of Biochemistry and Molecular Biology, Oregon Health Sciences University, Portland, Oregon 972011; Department of Microbiology, Louisiana State University Medical Center, New Orleans, Louisiana 701122; Dana-Farber Cancer Institute and Harvard Medical School3 and Howard Hughes Medical Institute,5 Boston, Massachusetts 02115; and Department of Molecular Cell Biology, The Weizmann Institute, Rehovot 76100, Israel4

Received 7 July 1998/Returned for modification 4 August 1998/Accepted 27 January 1999

The newly identified p53 homolog p73 can mimic the transcriptional activation function of p53. We investigated whether p73, like p53, participates in an autoregulatory feedback loop with MDM2. p73 bound to MDM2 both in vivo and in vitro. Wild-type but not mutant MDM2, expressed in human p53 null osteosarcoma Saos-2 cells, inhibited p73- and p53-dependent transcription driven by the MDM2 promoter-derived p53RE motif as measured in transient-transfection and chloramphenicol acetyltransferase assays and also inhibited p73-induced apoptosis in p53-null human lung adenocarcinoma H1299 cells. MDM2 did not promote the degradation of p73 but instead disrupted the interaction of p73, but not of p53, with p300/CBP by competing with p73 for binding to the p300/CBP N terminus. Both p73alpha and p73beta stimulated the expression of the endogenous MDM2 protein. Hence, MDM2 is transcriptionally activated by p73 and, in turn, negatively regulates the function of this activator through a mechanism distinct from that used for p53 inactivation.

* Corresponding author. Mailing address: Department of Biochemistry and Molecular Biology, Oregon Health Sciences University, 3181 SW Sam Jackson Park Rd., Portland, OR 97201. Phone: (503) 494-7414. Fax: (503) 494-8393. E-mail: LUH{at}OHSU.edu.

Molecular and Cellular Biology, May 1999, p. 3257-3266, Vol. 19, No. 5
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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