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Originally published In Press as doi:10.1074/jbc.C100008200 on February 13, 2001

J. Biol. Chem., Vol. 276, Issue 16, 12477-12480, April 20, 2001
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ACCELERATED PUBLICATION
Smurf1 Interacts with Transforming Growth Factor-beta Type I Receptor through Smad7 and Induces Receptor Degradation*

Takanori EbisawaDagger §, Minoru FukuchiDagger §, Gyo MurakamiDagger , Tomoki Chiba, Keiji Tanaka, Takeshi ImamuraDagger , and Kohei MiyazonoDagger ||**

From the Dagger  Department of Biochemistry, The Cancer Institute of the Japanese Foundation for Cancer Research, and Research for the Future Program, the Japan Society for the Promotion of Science, 1-37-1 Kami-ikebukuro, Toshima-ku, Tokyo 170-8455,  The Tokyo Metropolitan Institute of Medical Science, 3-18-22 Honkomagome, Bunkyo-ku, Tokyo 113-8613, and || Department of Molecular Pathology, Graduate School of Medicine, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan

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 (Tbeta R-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 Tbeta R-I via Smad7, with subsequent enhancement of turnover of Tbeta R-I and Smad7. These results thus reveal a novel function of Smad7, i.e. induction of degradation of Tbeta R-I through recruitment of an E3 ligase to the receptor.

* This research was supported by grants-in-aid for scientific research from the Ministry of Education, Science, Sports and Culture of Japan and by special coordination funds for promoting science and technology from the Science and Technology Agency of Japan.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ Contributed equally to this work.

** To whom correspondence should be addressed: Dept. of Biochemistry, The Cancer Inst. of the Japanese Foundation for Cancer Research, 1-37-1 Kami-ikebukuro, Toshima-ku, Tokyo 170-8455, Japan. Tel.: 81-3-5394-3866; Fax: 81-3-3918-0342; E-mail: miyazono-ind@ umin.ac.jp.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.


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