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Casein kinase 1 is a novel negative regulator of E-cadherin-based cell-cell contacts.: CK1 negatively regulates the E-cadherin complex

Abstract : Cadherins are the most crucial membrane proteins for the formation of tight and compact cell-cell contacts. Cadherin-based cell-cell adhesions are dynamically established and/or disrupted during various physiological and pathological processes. However, the molecular mechanisms that regulate cell-cell contacts are not fully understood. In this paper, we report a novel functional role of casein kinase 1 (CK1) in the regulation of cell-cell contacts. Firstly, we observed that IC261, a specific inhibitor of CK1, stabilizes cadherin-based cell-cell contacts, whereas the overexpression of CK1 disrupts them. CK1 colocalizes with E-cadherin and phosphorylates the cytoplasmic domain of E-cadherin in vitro and in a cell culture system. We show that the major CK1 phosphorylation site of E-cadherin is serine 846, a highly conserved residue between classical cadherins. Constitutively phosphorylated E-cadherin (S846D) is unable to localize at cell-cell contacts and has decreased adhesive activity. Furthermore, phosphorylated E-cadherin (S846D) has weaker interactions with beta-catenin and is internalized more efficiently than wild-type E-cadherin. These data indicate that CK1 is a novel negative regulator of cadherin-based cell-cell contacts.
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Submitted on : Friday, April 25, 2008 - 3:49:26 PM
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Sophie Dupre-Crochet, Angelica Figueroa, Catherine Hogan, Emma Ferber, Carl Uli Bialucha, et al.. Casein kinase 1 is a novel negative regulator of E-cadherin-based cell-cell contacts.: CK1 negatively regulates the E-cadherin complex. Molecular and Cellular Biology, American Society for Microbiology, 2007, 27 (10), pp.3804-16. ⟨10.1128/MCB.01590-06⟩. ⟨inserm-00275884⟩

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