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J Biol Chem, Vol. 273, Issue 36, 22865-22868, September 4, 1998
From the Cell Biology Program and Howard Hughes Medical Institute,
Memorial Sloan-Kettering Cancer Center, New York, New York 10021
SMADs are transforming growth factor 
(TGF-) receptor substrates and mediators of TGF- transcriptional
responses. Here we provide evidence that the coactivators p300 and CBP
interact with Smads 1 through 4. The biological relevance of this
interaction is shown in vivo by overexpression of the
adenovirus E1A protein and mutant forms of E1A that lack p300-binding
sites. Wild-type E1A, but not the mutants, inhibits
SMAD-dependent transcriptional responses to TGF-. E1A
also inhibits the intrinsic transactivating function of the Smad4 MH2
domain. In addition, overexpression of p300 enhances
SMAD-dependent transactivation. Our results suggest a role
for p300/CBP in SMAD-mediated transcriptional activation and provide an
explanation for the observed ability of E1A to interfere with TGF-
action.
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