The RING domain of PIASy is involved in the suppression of bone morphogenetic protein-signaling pathway.
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概要
- 論文の詳細を見る
Bone morphogenetic proteins (BMPs) play central roles in differentiation, development, and physiologic tissue remodeling. Recently, we have demonstrated that a protein inhibitor of activated STAT, PIASy, suppresses TGF-β signaling by interacting with Sma and MAD-related protein 3 (Smad3). In this study, we examined a PIASy-dependent inhibitory effect on BMP signaling. PIASy expression was induced by BMP-2 stimulation and suppressed BMP-2-dependent Smad activity in hepatoma cells. Furthermore, BMP-2-regulated Smads directly bound to PIASy. We also demonstrated that the RING domain of PIASy played an important role in PIASy-mediated suppression of Smad activity. We here provide evidence that the inhibitory action of PIASy on BMP-regulated Smad activity was due to direct physical interactions between Smads and PIASy through its RING domain.
- Elsevierの論文
- 2004-06-18
著者
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Shimoda Kazuya
九州大学 第1内科
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Yamamoto Yu
北海道大学 薬学研究院衛生化学
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Imoto Seiyu
Department Of Immunology Graduate School Of Pharmaceutical Sciences Hokkaido University
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Imoto Seiyu
北海道大学 大学院薬学研究科
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Shimoda Kazuya
Medicine And Biosystemic Science Graduate School Of Medical Sciences Kyushu University
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