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. 2017 May 11;10:140. doi: 10.3389/fnmol.2017.00140

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Copyright © 2017 Feilen, Haubrich, Strecker, Probst, Eggert, Stier, Sinning, Konietzko, Kins, Simon and Wild.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Physiological function of Fe65 dimerization. In a schematic model Fe65-mediated APP signaling is divided into four steps: (1) In the cytosol Fe65 forms a closed dimer by mimicking the AICD and thereby shielding the binding epitope. (2) APP binding at the cell membrane, putatively induced by phosphatidyl-inositol-4,5-bisphosphate (PIP₂)-mediated recruitment, opens the dimer and the AICD/Fe65-PTB2 interaction is formed. The AICD changes from a disordered to a structured conformation. (3) Upon secretase cleavage of APP, AICD-Fe65 signaling complexes translocate to the nucleus. (4) Respective transcription activation processes are initiated.