Junichi Shioi

TL;DR: It is shown that presenilin‐1 (PS1), a protein involved in Alzheimer's disease, controls a γ‐secretase‐like cleavage of E‐cadherin that stimulates disassembly of the E‐ cadher in– catenin complex and increases the cytosolic pool of β‐catenin, a key regulator of the Wnt signaling pathway.

TL;DR: It is shown that a PS1-dependent gamma-secretase protease activity promotes an epsilon-like cleavage of N-cadherin to produce its intracellular domain peptide, N-Cad/CTF2, which functions as a potent repressor of CBP/CREB-mediated transcription.

TL;DR: It is shown that PS1, a protein involved in familial Alzheimer's disease (FAD), promotes cell survival by activating the PI3K/Akt cell survival signaling, and this function of PS1 is unaffected by γ‐secretase inhibitors.

TL;DR: Together, data show that PS1 incorporates into the cadherin/catenin adhesion system and regulates cell-cell adhesion in MDCK cells and in brain, it forms complexes with both E and N-cadherin and concentrates at synaptic adhesions.

TL;DR: It is shown that presenilin-1 (PS1), a protein involved in Alzheimer's disease, binds directly to epithelial cadherin (E-cadherin), and this binding is mediated by the large cytoplasmic loop of PS1 and requires the membrane-proximal cytopalasmic sequence 604–615 of mature E-cADherin.