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J. Biol. Chem., Vol. 276, Issue 17, 14514-14523, April 27, 2001
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From the Department of Biochemistry and Molecular Biology, Mount
Sinai School of Medicine, New York, New York 10029-6574
To understand the role of the
Yes-associated protein (YAP), binding partners of its WW1 domain were
isolated by a yeast two-hybrid screen. One of the interacting proteins
was identified as p53-binding protein-2 (p53BP-2). YAP and p53BP-2
interacted in vitro and in vivo using their WW1
and SH3 domains, respectively. The YAP WW1 domain bound to the YPPPPY
motif of p53BP-2, whereas the p53BP-2 SH3 domain interacted with the
VPMRLR sequence of YAP, which is different from other known SH3
domain-binding motifs. By mutagenesis, we showed that this unusual SH3
domain interaction was due to the presence of three consecutive
tryptophans located within the
Yes-associated Protein and p53-binding Protein-2 Interact through
Their WW and SH3 Domains*
and
C strand of the SH3 domain. A
point mutation within this triplet, W976R, restored the binding
selectivity to the general consensus sequence for SH3 domains, the
PXXP motif. A constitutively active form of c-Yes was
observed to decrease the binding affinity between YAP and p53BP-2 using
chloramphenicol acetyltransferase/enzyme-linked immunosorbent
assay, whereas the overexpression of c-Yes did not modify
this interaction. Since overexpression of an activated form of c-Yes
resulted in tyrosine phosphorylation of p53BP-2, we propose that the
p53BP-2 phosphorylation, possibly in the WW1 domain-binding motif,
might negatively regulate the YAP·p53BP-2 complex.
*
This work was supported by Grants CA45757 and AR45626 from
the National Institutes of Health and by Grant RG0234 from the Human
Frontier Science Program Organization.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.
To whom correspondence should be addressed: Serono Pharmaceutical
Research Inst., 14, chemin des Aulx, Plan-Les-Ouates, 1228 Geneva,
Switzerland. Tel.: 41-22-706-9788; Fax: 41-22-794-6965; E-mail:
xavier.espanel@serono.com.
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