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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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Influence of APP on Fe65 dimerization. HEK cells expressing exogenous Fe65-HA, Fe65-Flag or APP-myc were subjected for subcellular fractionation. (A) The cytosolic and membrane fractions were separated on a BlueNative-Gel and analyzed by Western Blotting using 3F10 (anti HA) and SC789 (anti myc) antibodies. Note the shift of Fe65 from the cytosolic to the membrane fraction when co-expressed with APP. (B) Co-Immunoprecipitation (Co-IP) analysis of whole cell lysates (upper panel) and whole cell lysates and membrane fraction (lower panel) of HEK293 cells expressing Fe65-HA and Fe65-Flag alone or together with APP-myc. Cells expressing Fe65-HA and APP-myc served as positive and cells lacking Fe65-HA as negative control. For direct load 4% of the total extracts were loaded. Immunoprecipitation was carried out with anti-HA antibody covered beads. Immunoprecipitates were eluted by denaturation and probes were subjected for PAGE (8% Tris/glycine gels) and Western analysis using 3F10 (anti HA), SC789 (anti myc) and M2 (anti Flag) antibodies.