| First Author | Vinyoles M | Year | 2014 |
| Journal | Mol Cell | Volume | 53 |
| Issue | 3 | Pages | 444-57 |
| PubMed ID | 24412065 | Mgi Jnum | J:213018 |
| Mgi Id | MGI:5582693 | Doi | 10.1016/j.molcel.2013.12.010 |
| Citation | Vinyoles M, et al. (2014) Multivesicular GSK3 sequestration upon Wnt signaling is controlled by p120-catenin/cadherin interaction with LRP5/6. Mol Cell 53(3):444-57 |
| abstractText | The Wnt canonical ligands elicit the activation of beta-catenin transcriptional activity, a response dependent on, but not limited to, beta-catenin stabilization through the inhibition of GSK3 activity. Two mechanisms have been proposed for this inhibition, one dependent on the binding and subsequent block of GSK3 to LRP5/6 Wnt coreceptor and another one on its sequestration into multivesicular bodies (MVBs). Here we report that internalization of the GSK3-containing Wnt-signalosome complex into MVBs is dependent on the dissociation of p120-catenin/cadherin from this complex. Disruption of cadherin-LRP5/6 interaction is controlled by cadherin phosphorylation and requires the previous separation of p120-catenin; thus, p120-catenin and cadherin mutants unable to dissociate from the complex block GSK3 sequestration into MVBs. These mutants substantially inhibit, but do not completely prevent, the beta-catenin upregulation caused by Wnt3a. These results, besides elucidating how GSK3 is sequestered into MVBs, support this mechanism as cause of beta-catenin stabilization by Wnt. |
