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.
journal_name
J Cell Scijournal_title
Journal of cell scienceauthors
Casagolda D,Del Valle-Pérez B,Valls G,Lugilde E,Vinyoles M,Casado-Vela J,Solanas G,Batlle E,Reynolds AB,Casal JI,de Herreros AG,Duñach Mdoi
10.1242/jcs.067512subject
Has Abstractpub_date
2010-08-01 00:00:00pages
2621-31issue
Pt 15eissn
0021-9533issn
1477-9137pii
123/15/2621journal_volume
123pub_type
杂志文章abstract：:Normal human foreskin keratinocytes (HFKs) and transformed HFKs (FEPE1L-8 cells) generated by the introduction of cloned human papillomavirus type 16 sequences were compared for the expression and function of a family of adhesion receptors termed integrins. Initially, cells were examined in conventional monolayer cult...
journal_title：Journal of cell science
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journal_title：Journal of cell science
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