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The RING domain of PIASy is involved in the suppression of bone morphogenetic protein-signaling pathway.
Title: | The RING domain of PIASy is involved in the suppression of bone morphogenetic protein-signaling pathway. |
Authors: | Imoto, Seiyu Browse this author | Sugiyama, Kenji Browse this author | Yamamoto, Tetsuya Browse this author | Matsuda, Tadashi Browse this author →KAKEN DB |
Keywords: | BMP | Smad | RING domain | PIASy | Transcription |
Issue Date: | 18-Jun-2004 |
Publisher: | Elsevier |
Journal Title: | Biochemical and Biophysical Research Communications |
Volume: | 319 |
Issue: | 1 |
Start Page: | 275 |
End Page: | 282 |
Publisher DOI: | 10.1016/j.bbrc.2004.04.161 |
PMID: | 15158472 |
Abstract: | 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. |
Relation: | http://www.sciencedirect.com/science/journal/0006291X |
Type: | article (author version) |
URI: | http://hdl.handle.net/2115/28116 |
Appears in Collections: | 薬学研究院 (Faculty of Pharmaceutical Sciences) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
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Submitter: 松田 正
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