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. 2017 Sep 29;7:12456. doi: 10.1038/s41598-017-12334-2

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© The Author(s) 2017

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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FE65 T579 phosphorylation potentiates FE65-mediated APP processing. (A) HEK293 cells were co-transfected with GAL4-APP, pFR-Luc and phRL-TK together with EV, FE65, FE65 T579A or FE65 T579E. Phosphomimetic mutation of FE65 T579 further enhances the effect of FE65 on APP-GAL4 cleavage. n = 5. *P < 0.001. Results are means ± S.D. The expression of FE65 and the mutants were determined by immunoblotting. (B) Cells were transfected with APP + BACE1 + FE65/T579A/T579E. Transfected cell lysates were resolved on 16% Tris-Tricine gel, and immunoblotted for APP CTFs. Arrows denote CTF-α, -β or -β’. UT: untransfected. Two exposures of CTF blot were shown (C) Cells were transfected with APP together with EV, FE65, FE65 T579A or FE65 T579E. Levels of secreted Aβ1–40 (top graph) and 1–42 (bottom graph) were measured by corresponding Aβ ELISA kits. FE65 T579E phosphomimetic mutation potentiates FE65-mediated Aβ liberation. n = 5. *P < 0.001. Results are means ± S.D.