Physical and functional interaction of SMADS and p300/CBP Journal Article

  


Authors: Pouponnot, C.; Jayaraman, L.; Massagué, J.
Article Title: Physical and functional interaction of SMADS and p300/CBP
Abstract: SMADs are transforming growth factor β (TGF-β) receptor substrates and mediators of TGF-β 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-β. 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-β action.
Keywords: signal transduction; controlled study; protein expression; gene mutation; human cell; dna-binding proteins; nonhuman; protein domain; animal cell; gene overexpression; transforming growth factor beta; protein protein interaction; transcription initiation; protein binding; keratinocyte; animalia; nuclear proteins; transcription regulation; genetic transfection; cell culture; escherichia coli; recombinant proteins; transactivation; reporter gene; transforming growth factor beta receptor; trans-activators; acetyltransferases; adenoviridae; regulator protein; virus protein; adenovirus e1a proteins; lung alveolus epithelium; trans-activation (genetics); creb-binding protein; histone acetyltransferases; human; priority journal; article
Journal Title: Journal of Biological Chemistry
Volume: 273
Issue: 36
ISSN: 0021-9258
Publisher: American Society for Biochemistry and Molecular Biology  
Date Published: 1998-09-04
Start Page: 22865
End Page: 22868
Language: English
DOI: 10.1074/jbc.273.36.22865
PUBMED: 9722503
PROVIDER: scopus
DOI/URL:

https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032483493&doi=10.1074%2fjbc.273.36.22865&partnerID=40&md5=66d9d8aedd0cc7a84943821673adf4a0
Notes: Article -- Export Date: 12 December 2016 -- Source: Scopus
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MSK Authors
  1. Celio Pouponnot
    6 Pouponnot
  2. Joan Massague
    388 Massague
  3. Lata Jayaraman
    3 Jayaraman
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