A p120-catenin-CK1epsilon complex regulates Wnt signaling

p120-catenin is an E-cadherin-associated protein that modulates E-cadherin function and stability. We describe here that p120-catenin is required for Wnt pathway signaling. p120-catenin binds and is phosphorylated by CK1ε in response to Wnt3a. p120-catenin also associates to the Wnt co-receptor LRP5...

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Detalles Bibliográficos
Autores: Casagolda, David, Valle Pérez, Beatriz del, Valls, Gabriela, Lugilde, Ero, Vinyoles, Meritxell, Casado Vela, Juan, Solanas, Guiomar, Batlle Gómez, Eduard, Reynolds, Albert B., Casal, José Ignacio, García de Herreros, Antonio, Duñach, Mireia
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2010
País:España
Institución:Universitat Pompeu Fabra
Repositorio:Repositorio Digital de la UPF
OAI Identifier:oai:repositori.upf.edu:10230/25587
Acceso en línea:http://hdl.handle.net/10230/25587
http://dx.doi.org/10.1242/jcs.067512
Access Level:acceso abierto
Palabra clave:Proteïnes quinases -- Metabolisme
Cadherines
CK1
E-cadherin
Wnt
p120-catenin
Descripción
Sumario:p120-catenin is an E-cadherin-associated protein that modulates E-cadherin function and stability. We describe here that p120-catenin is required for Wnt pathway signaling. p120-catenin binds and is phosphorylated by CK1ε in response to Wnt3a. p120-catenin also associates to the Wnt co-receptor LRP5/6, an interaction mediated by E-cadherin, showing an unexpected physical link between adherens junctions and a Wnt receptor. Depletion of p120-catenin abolishes CK1ε binding to LRP5/6 and prevents CK1ε activation upon Wnt3a stimulation. Elimination of p120-catenin also inhibits early responses to Wnt, such as LRP5/6 and Dvl-2 phosphorylation and axin recruitment to the signalosome, as well as later effects, such as β-catenin stabilization. Moreover, since CK1ε is also required for E-cadherin phosphorylation, a modification that decreases the affinity for β-catenin, p120-catenin depletion prevents the increase in β-catenin transcriptional activity even in the absence of β-catenin degradation. Therefore, these results demonstrate a novel and crucial function of p120-catenin in Wnt signaling and unveil additional points of regulation by this factor of β-catenin transcriptional activity different of β-catenin stability.