| First Author | Sezaki T | Year | 2013 |
| Journal | FEBS Lett | Volume | 587 |
| Issue | 11 | Pages | 1624-9 |
| PubMed ID | 23624079 | Mgi Jnum | J:201272 |
| Mgi Id | MGI:5512917 | Doi | 10.1016/j.febslet.2013.04.015 |
| Citation | Sezaki T, et al. (2013) Dlg5 interacts with the TGF-beta receptor and promotes its degradation. FEBS Lett 587(11):1624-9 |
| abstractText | 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-beta (TGF-beta) signaling. However, the mechanism underlying the regulation of TGF-beta signaling is unclear. We show here that Dlg5 interacts and colocalizes with both TGF-beta type I (TbetaRI) and type II (TbetaRII) receptors at the plasma membrane. TbetaRI activation is not required for this interaction. Furthermore, the overexpression of Dlg5 enhances the degradation of TbetaRI. Proteasome inhibitors inhibited this enhanced degradation. These results suggest that Dlg5 interacts with TbetaRs and promotes their degradation. |
