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

被引：691

作者：

Ebisawa, T

Fukuchi, M

Murakami, G

Chiba, T

Tanaka, K

Imamura, T

Miyazono, K

机构：

[1] Japanese Fdn Canc Res, Inst Canc, Dept Biochem, Toshima Ku, Tokyo 1708455, Japan

[2] Japanese Fdn Canc Res, Res Future Program, Toshima Ku, Tokyo 1708455, Japan

[3] Tokyo Metropolitan Inst Med Sci, Bunkyo Ku, Tokyo 1138613, Japan

[4] Univ Tokyo, Dept Mol Pathol, Grad Sch Med, Bunkyo Ku, Tokyo 1130033, Japan

来源：

JOURNAL OF BIOLOGICAL CHEMISTRY | 2001年 / 276卷 / 16期

关键词：

D O I：

10.1074/jbc.C100008200

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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

引用

页码：12477 / 12480

页数：4

共 20 条

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