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つくばリポジトリ (Tulips-R) >
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Biochemical and biophysical research communications >
Please use this identifier to cite or link to this item:
http://hdl.handle.net/2241/101159
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| Title: | Roles of mono-ubiquitinated Smad4 in the formation of Smad transcriptional complexes |
| Authors: | Wang, Bei
Suzuki, Hiroyuki
Kato, Mitsuyasu
鈴木, 裕之
加藤, 光保 |
| Issue Date: | Nov-2008 |
| Publisher: | Elsevier Inc. |
| Journal Title: | Biochemical and Biophysical Research Communications |
| Volume: | 376 |
| Issue: | 2 |
| Start Page: | 288 |
| End Page: | 292 |
| DOI: | 10.1016/j.bbrc.2008.08.143 |
| PMID: | 18783722 |
| Abstract: | TGF-β activates receptor-regulated Smad (R-Smad) through phosphorylation by type I receptors. Activated R-Smad binds to Smad4 and the complex translocates into the nucleus and stimulates the transcription of target genes through association with co-activators including p300. It is not clear, however, how activated Smad complexes are removed from target genes. In this study, we show that TGF-β enhances the mono-ubiquitination of Smad4. Smad4 mono-ubiquitination was promoted by p300 and suppressed by the c-Ski co-repressor. Smad4 mono-ubiquitination disrupted the interaction with Smad2 in the presence of constitutively active TGF-β type I receptor. Furthermore, mono-ubiquitinated Smad4 was not found in DNA-binding Smad complexes. A Smad4-Ubiquitin fusion protein, which mimics mono-ubiquitinated Smad4, enhanced localization to the cytoplasm. These results suggest that mono-ubiquitination of Smad4 occurs in the transcriptional activator complex and facilitates the turnover of Smad complexes at target genes. |
| URI: | http://hdl.handle.net/2241/101159 |
| Rights: | © 2008 Elsevier Inc. |
| Text Version: | author |
| Appears in Collections: | Biochemical and biophysical research communications
加藤 光保 (Kato Mitsuyasu)
鈴木 裕之 (Suzuki Hiroyuki)
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