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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; Richardson, EC; (2007) Casein kinase 1 is a novel negative regulator of E-cadherin-based cell-cell contacts. Mol Cell Biol , 27 (10) pp. 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 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.

Type: Article
Title: Casein kinase 1 is a novel negative regulator of E-cadherin-based cell-cell contacts.
Location: United States
DOI: 10.1128/MCB.01590-06
Keywords: Amino Acid Sequence, Animals, Cadherins, Casein Kinase I, Cell Adhesion, Cells, Cultured, Endocytosis, Humans, Indoles, Intercellular Junctions, Isoenzymes, Molecular Sequence Data, Phloroglucinol, Phosphorylation, RNA Interference, Sequence Alignment, Serine, beta Catenin
UCL classification: UCL > School of Life and Medical Sciences
UCL > School of Life and Medical Sciences > Faculty of Life Sciences
URI: http://discovery.ucl.ac.uk/id/eprint/37277
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