Physical Interaction with Yes-associated Protein Enhances p73 Transcriptional Activity

Sabrina Strano, Eliana Munarriz, Mario Rossi, Luisa Castagnoli, Yosef Shaul, Ada Sacchi, Moshe Oren, Marius Sudol, Gianni Cesareni, Giovanni Blandino

Research output: Contribution to journalArticlepeer-review


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 p73α, p73β, and p63α, which bind to YAP, the endogenous as well as exogenously expressed wild-type p53 (wt-p53) and the p73γ 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 p73α transcriptional activity. Differential interaction of YAP with members of the p53 family may provide a molecular explanation for their functional divergence in signaling.

Original languageEnglish
Pages (from-to)15164-15173
Number of pages10
JournalJournal of Biological Chemistry
Issue number18
Publication statusPublished - May 4 2001

ASJC Scopus subject areas

  • Biochemistry


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