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. 2020 Sep 4;8:154. doi: 10.1186/s40478-020-01001-9

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© The Author(s) 2020

Open AccessThis 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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

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Fig. 8 — Analysis of a putative second dimerization region in FLNc. a Yeast-two-hybrid experiments investigating interaction of FLNc Ig-like domains 15–23 (prey) with different fragments of FLNc as baits. Interaction was found with d15–23, d18–21 and d19–21 of FLNc. Note that deletion of the FLNc specific insertion in Ig-like domain 20 (d19–21Δ) abolished the interaction. +: interaction; −: no interaction. b FLNc d18–21 with and without (Δ) insertion in d20, and FLNa d18–21 were incubated in the presence of the cross linker EGS. Separation by PAGE and western blotting with an antibody against the immunotag of the recombinant fragments indicated oligomerization of FLNc d18–21 (arrow) but not of the other constructs. c GST pull down assay indicating that GST-FLNc d19–21 (GST + FLNc) binds T7-tagged FLNc d19–21, but not T7-tagged FLNc d15–17. GST alone does not bind any of the FLNc fragments. lc: loading control showing the correct size of the FLNc fragments