Vinyoles, MeritxellValle Pérez, Beatriz delCurto, JosuéViñas Castells, Rosa, 1985-Alba Castellón, Lorena, 1984-García de Herreros, AntonioDuñach, Mireia2015-06-152015-06-152014Vinyoles M, DelValle-Párez B, Curto J, Viñas-Castells R, Alba-Castellón L, Garcia de Herreros A et al. Multivesicular GSK3 sequestration upon wnt signaling is controlled by p120-catenin/cadherin interaction with LRP5/6. Molecular cell. 2014;53(3):444-57. DOI: 10.1016/j.molcel.2013.12.0101097-2765http://hdl.handle.net/10230/23820The Wnt canonical ligands elicit the activation of β-catenin transcriptional activity, a response dependent on, but not limited to, β-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 β-catenin upregulation caused by Wnt3a. These results, besides elucidating how GSK3 is sequestered into MVBs, support this mechanism as cause of β-catenin stabilization by Wnt.application/pdfeng© Elsevier This is the published version of an article http://dx.doi.org/10.1016/j.molcel.2013.12.010 that appeared in the journal Molecular cell. It is published in an Open Archive under an Elsevier user license. Details of this licence are available here: http://www.elsevier.com/about/open-access/open-access-policies/oa-license-policy/elsevier-user-licenseFosforilacióMultivesicular GSK3 sequestration upon wnt signaling is controlled by p120-catenin/cadherin interaction with LRP5/6info:eu-repo/semantics/articlehttp://dx.doi.org/10.1016/j.molcel.2013.12.010info:eu-repo/semantics/openAccess