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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, Catherine, Ferber, E. C., Bialucha, C. U., Adams, J., Richardson, E. C. N. and Fujita, Y. 2007. Casein Kinase 1 Is a novel negative regulator of E-cadherin-based cell-cell contacts. Molecular and Cellular Biology 27 (10) , pp. 3804-3816. 10.1128/MCB.01590-06

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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.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Biosciences
European Cancer Stem Cell Research Institute (ECSCRI)
Publisher: American Society for Microbiology
ISSN: 0270-7306
Last Modified: 04 Jun 2017 06:39

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