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. 2019 Mar 6;9:3716. doi: 10.1038/s41598-019-39884-x

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© The Author(s) 2019

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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Deletion of the third FNIII domain increases the accessibility to the fourth FNIII domain. (a) Model for control of L1 proteolysis by conformational changes within the FNIII domains. (b) The accessibility of an antibody targeting the membrane proximal fourth FNIII domain for deletion mutants of L1cam in which the first three FNIII domains were deleted individually was analyzed by flow cytometry. The ratio of the mean fluorescence intensity for cells stained with an antibody targeting the fourth FNIII domain (UJ127-11) was given relative to the mean fluorescence intensity obtained for an antibody targeting the second Ig-domain in the N-terminal (5G3). Mean values +/− SEM for at least three independent experiments are plotted. Example histograms and dot-plots are displayed in Supplemental Fig. 4. Statistical significance was assessed by one-way ANOVA followed by Dunnett’s multiple comparison test.