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| ファイル | 記述 | サイズ | フォーマット | |
|---|---|---|---|---|
| j.febslet.2013.04.015.pdf | 863.87 kB | Adobe PDF | 見る/開く |
| タイトル: | Dlg5 interacts with the TGF-β receptor and promotes its degradation. |
| 著者: | Sezaki, Takuhito Tomiyama, Lucia Kimura, Yasuhisa  Ueda, Kazumitsu   https://orcid.org/0000-0003-2980-6078 (unconfirmed)Kioka, Noriyuki https://orcid.org/0000-0002-2708-537X (unconfirmed) |
| 著者名の別形: | 木岡, 紀幸 |
| キーワード: | Discs large homolog 5 TGF-β receptor Protein degradation Crohn’s disease Epithelial to mesenchymal transition |
| 発行日: | 5-Jun-2013 |
| 出版者: | Elsevier B.V. |
| 誌名: | FEBS letters |
| 巻: | 587 |
| 号: | 11 |
| 開始ページ: | 1624 |
| 終了ページ: | 1629 |
| 抄録: | Discs large homolog 5 (Dlg5) is a member of the membrane-associated guanylate kinase adaptor family of proteins and is involved in epithelial-to-mesenchymal transition via transforming growth factor-β (TGF-β) signaling. However, the mechanism underlying the regulation of TGF-β signaling is unclear. We show here that Dlg5 interacts and colocalizes with both TGF-β type I (TβRI) and type II (TβRII) receptors at the plasma membrane. TβRI activation is not required for this interaction. Furthermore, the overexpression of Dlg5 enhances the degradation of TβRI. Proteasome inhibitors inhibited this enhanced degradation. These results suggest that Dlg5 interacts with TβRs and promotes their degradation. |
| 著作権等: | © 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. |
| URI: | http://hdl.handle.net/2433/175271 |
| DOI(出版社版): | 10.1016/j.febslet.2013.04.015 |
| PubMed ID: | 23624079 |
| 出現コレクション: | 学術雑誌掲載論文等 |
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