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A p120-catenin/CK1ε complex regulates Wnt signalin

AuthorsCasagolda, David; Valle-Perez, Beatriz del; Valls, Gabriela; Lugilde, Ero; Vinyoles, Meritxell; Casado-Vela, Juan; Solanas, Guiomar; Batlle, Eduard; Reynolds, Albert B.; Casal, J. Ignacio ; García de Herreros, Antonio; Duñach, Mireia
Issue Date1-Aug-2010
PublisherCompany of Biologists
CitationJournal of Cell Science, 123 : 2621-2631 (2010)
Abstractp120-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
Description11 páginas, 7 figuras -- PAGS nros. 2621-2631
Publisher version (URL)http://dx.doi.org/10.1242/​jcs.067512
Appears in Collections:(CIB) Artículos
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