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Originally published In Press as doi:10.1074/jbc.M010484200 on January 24, 2001

J. Biol. Chem., Vol. 276, Issue 18, 15164-15173, May 4, 2001
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Physical Interaction with Yes-associated Protein Enhances p73 Transcriptional Activity*

Sabrina StranoDagger §, Eliana MunarrizDagger §, Mario Rossi||, Luisa Castagnoli||, Yosef Shaul**, Ada SacchiDagger , Moshe OrenDagger Dagger , Marius Sudol§§, Gianni Cesareni||, and Giovanni BlandinoDagger ¶¶

From the Dagger  Molecular Oncogenesis Laboratory, Regina Elena Cancer Institute, Rome 00158, Italy, || Department of Biology, University of Tor Vergata, Rome 00133, Italy, the Departments of ** Molecular Genetics and Dagger Dagger  Cell Biology, The Weizmann Institute of Science, Rehovot 76100, Israel, and the §§ Department of Medicine, Mount Sinai School of Medicine, New York, New York 10029-6574

Specific protein-protein interactions are involved in a large number of cellular processes and are mainly mediated by structurally and functionally defined domains. Here we report that the nuclear phosphoprotein p73 can engage in a physical association with the Yes-associated protein (YAP). This association occurs under physiological conditions as shown by reciprocal co-immunoprecipitation of complexes from lysates of P19 cells. The WW domain of YAP and the PPPPY motif of p73 are directly involved in the association. Furthermore, as required for ligands to group I WW domains, the terminal tyrosine (Y) of the PPPPY motif of p73 was shown to be essential for the association with YAP. Unlike p73alpha , p73beta , and p63alpha , which bind to YAP, the endogenous as well as exogenously expressed wild-type p53 (wt-p53) and the p73gamma isoform do not interact with YAP. Indeed, we documented that YAP interacts only with those members of the p53 family that have a well conserved PPXY motif, a target sequence for WW domains. Overexpression of YAP causes an increase of p73alpha transcriptional activity. Differential interaction of YAP with members of the p53 family may provide a molecular explanation for their functional divergence in signaling.

* This work was supported by Telethon-Italy Grant 369/bi (to G. B.), Associazione Italiana per la Ricerca sul Cancro Telethon and the Consiglio Nazionale delle Ricerche target project in Biotechnology (to G. C.), and by Human Frontier Science Program Organization Grant RG0234 and National Institutes of Health Grants AR45626 and CA45757 (to M. S.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ These authors contributed equally to this work.

Supported by European Community Grant QLG1-1999-00273.

¶¶ To whom correspondence should be addressed: Molecular Oncogenesis Laboratory, Regina Elena Cancer Institute, Via delle Messi d'Oro 156, Rome 00158, Italy. Tel.: 39-06-49852563; Fax: 39-06-49852505; E-mail: blandino@ifo.it.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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