Partnership between DPC4 and SMAD proteins in TGF-β signalling pathways Journal Article


Authors: Lagna, G.; Hata, A.; Hemmati-Brivanlou, A.; Massagué, J.
Article Title: Partnership between DPC4 and SMAD proteins in TGF-β signalling pathways
Abstract: THE TGF-β/activin/BMP superfamily of growth factors signals through heteromeric receptor complexes of type I and type II serine/threonine kinase receptors. The signal originated by TGF-β-like molecules appears to be transduced by a set of evolutionarily conserved proteins known as SMADs, which upon activation directly translocate to the nucleus where they may activate transcription. Five SMAD proteins have so far been characterized in vertebrates. These factors are related to the mediator of decapentaplegic (dpp) signalling, mothers against dpp (Mad), in Drosophila and to the Sma genes from Caenorhabditis elegans. Smad1 and Smad2 have been shown to mimic the effects of BMP and activin, respectively, both in Xenopus and in mammalian cells, whereas Smad3 (a close homologue of Smad2) and the related protein DPC4, a tumour-suppressor gene product, mediate TGF-β actions. We report here that DPC4 is essential for the function of Smad1 and Smad2 in pathways that signal mesoderm induction and patterning in Xenopus embryos, as well as antimitogenic and transcriptional responses in breast epithelial cells. DPC4 associates with Smad1 in response to BMP and with Smad2 in response to activin or TGF-β. DPC4 is therefore a regulated partner of SMADs that function in different signalling pathways of the TGF-β family.
Keywords: signal transduction; controlled study; unclassified drug; oncoprotein; human cell; dna-binding proteins; nonhuman; animal cell; oocyte; mammalia; animals; bone morphogenetic protein; smad protein; smad1 protein; transforming growth factor beta; embryo; protein protein interaction; cell line; transcription factor; transfection; phosphorylation; animalia; transcription factors; vertebrata; cloning, molecular; embryo, nonmammalian; tumor suppressor gene; breast epithelium; trans-activators; caenorhabditis elegans; repressor proteins; mesoderm; xenopus; growth substances; basic helix-loop-helix leucine zipper transcription factors; smad4 protein; embryonic induction; xenopus proteins; activin; activins; humans; human; priority journal; article; inhibins; oncoprotein dpc 4
Journal Title: Nature
Volume: 383
Issue: 6603
ISSN: 0028-0836
Publisher: Nature Publishing Group  
Date Published: 1996-10-31
Start Page: 832
End Page: 836
Language: English
DOI: 10.1038/383832a0
PUBMED: 8893010
PROVIDER: scopus
DOI/URL:
Notes: Article -- Export Date: 22 November 2017 -- Source: Scopus
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  1. Joan Massague
    388 Massague
  2. Akiko   Hata
    9 Hata