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Papers In Press, published online ahead of print February 13, 2001
Biochemistry, The JFCR Cancer Institute, Tokyo 170-8455
Corresponding Author: miyazono-ind{at}umin.ac.jp
Smad7 is an inhibitory Smad (I-Smad) which acts as a negative regulator of signaling by the transforming growth factor-b (TGF-b) superfamily proteins. Smad7 is induced by TGF-b, stably interacts with activated TGF-b type I receptor (TbR-I), and interferes with the phosphorylation of receptor-regulated Smads (R-Smads). Here we show that Smurf1, an E3 ubiquitin ligase for bone morphogenetic protein (BMP)-specific Smads, also interacts with Smad7 and induces Smad7-ubiquitination and -translocation into the cytoplasm. In addition, Smurf1 associates with TbR-I via Smad7, with subsequent enhancement of turnover of TbR-I and Smad7. These results thus reveal a novel function of Smad7, i.e., induction of degradation of TbR-I through recruitment of an E3 ligase to the receptor.
J. Biol. Chem, 10.1074/jbc.C100008200
Submitted on January 8, 2001
Revised on February 2, 2001
Accepted on February 12, 2001
Smurf1 Interacts with Transforming Growth Factor-b Type I Receptor through Smad7 and Induces Receptor Degradation
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