| First Author | Lee HJ | Year | 2015 |
| Journal | Elife | Volume | 4 |
| Pages | e08142 | PubMed ID | 26297804 |
| Mgi Jnum | J:226824 | Mgi Id | MGI:5698608 |
| Doi | 10.7554/eLife.08142 | Citation | Lee HJ, et al. (2015) Conformational change of Dishevelled plays a key regulatory role in the Wnt signaling pathways. Elife 4 |
| abstractText | The intracellular signaling molecule Dishevelled (Dvl) mediates canonical and non-canonical Wnt signaling via its PDZ domain. Different pathways diverge at this point by a mechanism that remains unclear. Here we show that the peptide-binding pocket of the Dvl PDZ domain can be occupied by Dvl's own highly conserved C-terminus, inducing a closed conformation. In Xenopus, Wnt-regulated convergent extension (CE) is readily affected by Dvl mutants unable to form the closed conformation than by wild-type Dvl. We also demonstrate that while Dvl cooperates with other Wnt pathway elements to activate canonical Wnt signaling, the open conformation of Dvl more effectively activates Jun N-terminal kinase (JNK). These results suggest that together with other players in the Wnt signaling pathway, the conformational change of Dvl regulates Wnt stimulated JNK activity in the non-canonical Wnt signaling. |
