A p120-catenin-CK1ε complex regulates Wnt signaling

David Casagolda, Beatriz Del Valle-Pérez, Gabriela Valls, Ero Lugilde, Meritxell Vinyoles, Juan Casado-Vela, Guiomar Solanas, Eduard Batlle, Albert B. Reynolds, José Ignacio Casal, Antonio García De Herreros, Mireia Duñach

Research output: Contribution to journalArticleResearchpeer-review

50 Citations (Scopus)


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.
Original languageEnglish
Pages (from-to)2621-2631
JournalJournal of Cell Science
Publication statusPublished - 1 Aug 2010


  • CK1ε
  • E-cadherin
  • Wnt
  • p120-catenin


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