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Smurf1 interacts with transforming growth factor-beta type I receptor through Smad7 and induces receptor degradation.

Smad7 is an inhibitory Smad that acts as a negative regulator of signaling by the transforming growth factor-beta (TGF-beta) superfamily proteins. Smad7 is induced by TGF-beta, stably interacts with activated TGF-beta type I receptor (TbetaR-I), and interferes with the phosphorylation of receptor-regulated Smads. Here we show that Smurf1, an E3 ubiquitin ligase for bone morphogenetic protein-specific Smads, also interacts with Smad7 and induces Smad7 ubiquitination and translocation into the cytoplasm. In addition, Smurf1 associates with TbetaR-I via Smad7, with subsequent enhancement of turnover of TbetaR-I and Smad7. These results thus reveal a novel function of Smad7, i.e. induction of degradation of TbetaR-I through recruitment of an E3 ligase to the receptor.

Pubmed ID: 11278251


  • Ebisawa T
  • Fukuchi M
  • Murakami G
  • Chiba T
  • Tanaka K
  • Imamura T
  • Miyazono K


The Journal of biological chemistry

Publication Data

April 20, 2001

Associated Grants


Mesh Terms

  • Activin Receptors, Type I
  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • COS Cells
  • Cell Line
  • Cercopithecus aethiops
  • DNA-Binding Proteins
  • Epithelial Cells
  • Humans
  • Ligases
  • Mink
  • Protein-Serine-Threonine Kinases
  • Receptors, Transforming Growth Factor beta
  • Recombinant Proteins
  • Sequence Alignment
  • Signal Transduction
  • Smad6 Protein
  • Smad7 Protein
  • Trans-Activators
  • Transfection
  • Transforming Growth Factor beta
  • Ubiquitin-Protein Ligases