Reference - Detail
| RRC ID | 44414 |
|---|---|
| Author | Sezaki T, Tomiyama L, Kimura Y, Ueda K, Kioka N. |
| Title | Dlg5 interacts with the TGF-β receptor and promotes its degradation. |
| Journal | FEBS Lett |
| 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. |
| Volume | 587(11) |
| Pages | 1624-9 |
| Published | 2013-6-5 |
| DOI | 10.1016/j.febslet.2013.04.015 |
| PII | S0014-5793(13)00301-3 |
| PMID | 23624079 |
| MeSH | Caco-2 Cells Cell Membrane / metabolism HEK293 Cells Humans Membrane Proteins / metabolism* Protein Binding Protein Serine-Threonine Kinases / metabolism* Protein Transport Proteolysis* Receptor, Transforming Growth Factor-beta Type I Receptor, Transforming Growth Factor-beta Type II Receptors, Transforming Growth Factor beta / metabolism* Transforming Growth Factor beta / physiology Tumor Suppressor Proteins / metabolism* |
| IF | 3.057 |
| Times Cited | 12 |
| WOS Category | BIOPHYSICS BIOCHEMISTRY & MOLECULAR BIOLOGY CELL BIOLOGY |
| Resource | |
| Human and Animal Cells | CACO-2(RCB0988) |