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

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

Electric-field-induced lifting of the valley degeneracy in alpha-(BEDT-TTF)_2I_3 Dirac-like Landau levels

The relativistic Landau levels in the layered organic material alpha-(BEDT-TTF)_2I_3 [BEDT-TTF=bis(ethylenedithio)tetrathiafulvalene] are sensitive to the tilt of the Dirac cones, which, as in the case of graphene, determine the low-energy electronic properties under appropriate pressure. We show that an applied inplane electric field, which happens to be in competition with the tilt of the cones, lifts the twofold valley degeneracy due to a different level spacing. The scenario may be tested in infrared transmission spectroscopy.Comment: 4 pages, 1 figure; version with minor corrections published in EP