Physical Interaction with Yes-associated Protein Enhances p73 Transcriptional Activity*

By S. Strano, E. Munarriz, Mario Rossi, L. Castagnoli, Y. Shaul, A. Sacchi, Moshe Oren, M. Sudol, G. Cesareni, G. Blandino. Journal of Biological Chemistry, 2001

247 citations recorded by the source corpus.

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 PPPPYmotif 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.

Subfields: Cell Biology, Molecular Biology, Oncology

View Paper: https://www.semanticscholar.org/paper/83c4f7d1ec4cc1aa54c1a9d03784381c5d1b35c9

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Citations in the corpus

The Hippo Signaling Pathway in Development and Cancer (2010, background): “Lastly, Ds and Fj have opposite effects on Ft-dependent PCP signaling (and are indeed expressed in opposing gradients in many tissues) (Casal et al., 2002; Strutt and Strutt, 2002; Yang et al., 2002) but have similar effects on Ft-dependent Hippo signaling (Rogulja et al.”
The Salvador–Warts–Hippo pathway — an emerging tumour-suppressor network (2007, background): “YKI has an acidic domain, which is required for its activity as a transcriptional co-activato”
Hippo signaling in organ size control. (2007, background): “YAP, the mammalian homolog of Yki, has been reported to function as the coactivator for several transcription factors, such as the p53 family member p73, the Runt family member PEBP2 , and the four TEAD/TEF transcription factors (Yagi et al. 1999; Strano et al. 2001; Vassilev et al. 2001).”
The Hippo pathway: regulators and regulations. (2013, background): “1999), p63/p73 (Strano et al. 2001), and ErbB4 (Komuro et al.”