Ferber, EC; Kajita, M; Wadlow, A; Tobiansky, L; Niessen, C; Ariga, H; Daniel, J; Ferber, EC; Kajita, M; Wadlow, A; Tobiansky, L; Niessen, C; Ariga, H; Daniel, J; Fujita, Y; - view fewer (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.

Preview

PDF J._Biol._Chem.-2008-Ferber-12691-700.pdf Download (887kB)

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.

Download activity - last month

Export as XMLCSVJSON

Download activity - last 12 months

Export as CSVXMLJSON

Downloads by country - last 12 months

Export as XMLCSVJSON

Archive Staff Only

View Item