Physical and functional interaction of SMADs and p300/CBP

被引：289

作者：

Pouponnot, C

Jayaraman, L

Massagué, J

机构：

[1] Mem Sloan Kettering Canc Ctr, Cell Biol Program, New York, NY 10021 USA

[2] Mem Sloan Kettering Canc Ctr, Howard Hughes Med Inst, New York, NY 10021 USA

来源：

JOURNAL OF BIOLOGICAL CHEMISTRY | 1998年 / 273卷 / 36期

关键词：

D O I：

10.1074/jbc.273.36.22865

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

SMADs are transforming growth factor beta (TGF-beta) receptor substrates and mediators of TGF-beta 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 EIA, but not the mutants, inhibits SMAD-dependent transcriptional responses to TGF-beta. 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-beta action.

引用

页码：22865 / 22868

页数：4

共 51 条

[1] TRANSFORMING GROWTH FACTOR-BETA-1 (TGF-BETA-1) REDUCES CELLULAR-LEVELS OF P34CDC2, AND THIS EFFECT IS ABROGATED BY ADENOVIRUS INDEPENDENTLY OF THE E1A-ASSOCIATED PRB BINDING-ACTIVITY [J].