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Casein kinase 1 is a novel negative regulator of E-cadherin-based cell-cell contacts

Dupre-Crochet, S; Figueroa, A; Hogan, C; Ferber, EC; Bialucha, CU; Adams, J; ... Fujita, Y; + view all (2007) Casein kinase 1 is a novel negative regulator of E-cadherin-based cell-cell contacts. Molecular and Cellular Biology , 27 (10) 3804 - 3816. 10.1128/MCB.01590-06.

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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 β-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. Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Type:Article
Title:Casein kinase 1 is a novel negative regulator of E-cadherin-based cell-cell contacts
DOI:10.1128/MCB.01590-06

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