| Literature DB >> 11278251 |
T Ebisawa1, M Fukuchi, G Murakami, T Chiba, K Tanaka, T Imamura, K Miyazono.
Abstract
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.Entities:
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Year: 2001 PMID: 11278251 DOI: 10.1074/jbc.C100008200
Source DB: PubMed Journal: J Biol Chem ISSN: 0021-9258 Impact factor: 5.157