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A role for the cleaved cytoplasmic domain of E-cadherin in the nucleus

Ferber, EC; Kajita, M; Wadlow, A; Tobiansky, L; Niessen, C; Ariga, H; Daniel, J; (2008) A role for the cleaved cytoplasmic domain of E-cadherin in the nucleus. Journal of Biological Chemistry , 283 (19) 12691 -12700. 10.1074/jbc.M708887200. Green open access

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Abstract

Cell-cell contacts play a vital role in intracellular signaling, although the molecular mechanisms of these signaling pathways are not fully understood. E-cadherin, an important mediator of cell-cell adhesions, has been shown to be cleaved by γ-secretase. This cleavage releases a fragment of E-cadherin, E-cadherin C-terminal fragment 2 (E-cad/CTF2), into the cytosol. Here, we study the fate and function of this fragment. First, we show that coexpression of the cadherin-binding protein, p120 catenin (p120), enhances the nuclear translocation of E-cad/CTF2. By knocking down p120 with short interfering RNA, we also demonstrate that p120 is necessary for the nuclear localization of E-cad/CTF2. Furthermore, p120 enhances and is required for the specific binding of E-cad/CTF2 to DNA. Finally, we show that E-cad/CTF2 can regulate the p120-Kaiso-mediated signaling pathway in the nucleus. These data indicate a novel role for cleaved E-cadherin in the nucleus.

Type: Article
Title: A role for the cleaved cytoplasmic domain of E-cadherin in the nucleus
Open access status: An open access version is available from UCL Discovery
DOI: 10.1074/jbc.M708887200
Publisher version: http://dx.doi.org/10.1074/jbc.M708887200
Language: English
Additional information: This research was originally published in Journal of Biological Chemistry. Emma C. Ferber, Mihoko Kajita, Anthony Wadlow, Lara Tobiansky, Carien Niessen, Hiroyoshi Ariga, Juliet Daniel, and Yasuyuki Fujita. A role for the cleaved cytoplasmic domain of E-cadherin in the nucleus. Journal of Biological Chemistry. 2008; 283:12691-12700. © the American Society for Biochemistry and Molecular Biology.
URI: http://discovery.ucl.ac.uk/id/eprint/26079
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