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. 2020 Nov 3;26(10):5592–5607. doi: 10.1038/s41380-020-00926-w

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© The Author(s) 2020, corrected publication 2020

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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Fig. 4 — a Immunofluorescence images showing the presence of APP and FERMT2 within the axonal growth cone stained with SiR-Actin. The right panel shows the presence of PLA-FERMT2/APP puncta within the axonal growth cone. b Impact of lentiviral transduction of nontargeting shRNA (shNT) or shRNA against FERMT2 (shFERMT2) on growth cone area, angular dispersion and speed of the actin-retrograde flow, and APP immunostaining. c Co-IP between endogenous APP and FERMT2 from membrane extracts of hippocampal PNC. Protein extracts were incubated with beads only, a mouse (Ms) antibody against APP (4G8), or a nonrelevant (NR) antibody. d APP pull-down experiment with wild-type (WT) or mutated (QW) FERMT2. Protein extracts from HeLa cells overexpressing FERMT2^WT or FERMT^QW were incubated with recombinant APP C-terminal fragment (C100). e The domain organization of FERMT2 protein (upper panel). Q614A/W615A (QW) mutation was reported to abolish the interaction of F3 domain of FERMT2 with the NxTY motif. The structural model of the FERMT2-APP complex (lower panel) was built by homology using the crystal structure of the FERMT2-Integrin-β3-tail complex [32]. f The impact of FERMT2 on APP metabolism in HEK293-APP^695WT cells is reverted with the overexpression of FERMT2^QW compared to FERMT2^WT. Scale bar = 5 µm. Mann–Whitney test; *p < 0.05.