INVESTIGADORES
MUNARRIZ Eliana Rosa
artículos
Título:
Physical interaction with Yes-associated protein enhances p73 transcriptional activity.
Autor/es:
STRANO S, MUNARRIZ E, ROSSI M, CASTAGNOLI L, SHAUL Y, SACCHI A, OREN M, SUDOL M, CESARENI G, BLANDINO G.
Revista:
JOURNAL OF BIOLOGICAL CHEMISTRY
Editorial:
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Referencias:
Año: 2001 p. 15164 - 15173
ISSN:
0021-9258
Resumen:
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.