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A role for the cleaved cytoplasmic domain of E-cadherin in the nucleus.
Journal of Biological Chemistry
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.
|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|
|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.|
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