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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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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.[1]

References

  1. Smurf1 interacts with transforming growth factor-beta type I receptor through Smad7 and induces receptor degradation. Ebisawa, T., Fukuchi, M., Murakami, G., Chiba, T., Tanaka, K., Imamura, T., Miyazono, K. J. Biol. Chem. (2001) [Pubmed]
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