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                  <mods:namePart>Casagolda, David</mods:namePart>
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                  <mods:namePart>Valle Pérez, Beatriz del</mods:namePart>
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                  <mods:namePart>Valls, Gabriela</mods:namePart>
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                  <mods:namePart>Casado Vela, Juan</mods:namePart>
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                  <mods:namePart>Batlle Gómez, Eduard</mods:namePart>
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                  <mods:namePart>Reynolds, Albert B.</mods:namePart>
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                  <mods:namePart>Casal, José Ignacio</mods:namePart>
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                  <mods:namePart>García de Herreros, Antonio</mods:namePart>
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               <mods:name>
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                  <mods:namePart>Duñach, Mireia</mods:namePart>
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                  <mods:dateIssued encoding="iso8601">2016-01-15T19:41:45Z2016-01-15T19:41:45Z2010</mods:dateIssued>
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               <mods:abstract>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.This study was supported by grants awarded by the Ministerio de Ciencia e Innovación: BFU2006-03203 and BFU2009-07578 to M.D. and SAF2006-00339 to A.G.H. Partial support from the Instituto Carlos III (RD06/0020/0040) and the Generalitat de Catalunya (2009SGR867 and 2009SGR585) is also appreciated. D.C. and G.V. were supported by predoctoral fellowships from the Ministerio de Educación and E.L., from the UAB.</mods:abstract>
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               <mods:accessCondition type="useAndReproduction">© Company of Biologists http://jcs.biologists.org/content/joces/123/15/2621.full.pdf DOI 10.1242/jcs.067512 info:eu-repo/semantics/openAccess</mods:accessCondition>
               <mods:subject>
                  <mods:topic>Proteïnes quinases -- Metabolisme</mods:topic>
               </mods:subject>
               <mods:subject>
                  <mods:topic>Cadherines</mods:topic>
               </mods:subject>
               <mods:subject>
                  <mods:topic>CK1</mods:topic>
               </mods:subject>
               <mods:subject>
                  <mods:topic>E-cadherin</mods:topic>
               </mods:subject>
               <mods:subject>
                  <mods:topic>Wnt</mods:topic>
               </mods:subject>
               <mods:subject>
                  <mods:topic>p120-catenin</mods:topic>
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                  <mods:title>A p120-catenin-CK1epsilon complex regulates Wnt signaling</mods:title>
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