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| File | Description | Size | Format | |
|---|---|---|---|---|
| j.febslet.2013.04.015.pdf | 863.87 kB | Adobe PDF | View/Open |
| Title: | Dlg5 interacts with the TGF-β receptor and promotes its degradation. |
| Authors: | 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) |
| Author's alias: | 木岡, 紀幸 |
| Keywords: | Discs large homolog 5 TGF-β receptor Protein degradation Crohn’s disease Epithelial to mesenchymal transition |
| Issue Date: | 5-Jun-2013 |
| Publisher: | Elsevier B.V. |
| Journal title: | FEBS letters |
| Volume: | 587 |
| Issue: | 11 |
| Start page: | 1624 |
| End page: | 1629 |
| Abstract: | 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. |
| Rights: | © 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. |
| URI: | http://hdl.handle.net/2433/175271 |
| DOI(Published Version): | 10.1016/j.febslet.2013.04.015 |
| PubMed ID: | 23624079 |
| Appears in Collections: | Journal Articles |
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