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. 2021 Jan 25;4:114. doi: 10.1038/s42003-020-01618-5

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© The Author(s) 2021

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. 6 — a Direct interactions between EGFR and CS-C (EGFR-CS) in primary C6st-1 WT, C6st-1 HE, and C6st-1 KO keratinocytes were examined by proximity ligation assay (PLA assay) using CS56 (anti-CS-C antibody) and anti-EGFR antibody. Keratinocytes digested with chondroitinase ABC were used as controls. b EGFR homodimers in primary keratinocytes were examined by PLA assay using anti-EGFR antibody. As a control, keratinocytes were digested with chondroitinase ABC, subjected to PLA assay. c The graph shows means ± S.D. of EGFR-CS signals (green dots)/cell counted in 7–12 cells from three independent experiments. d The graph shows means ± S.D. of EGFR homodimer signals (green dots)/cell counted in 7–12 cells from three independent experiments. Values are mean ± S.D. Statistical significance was determined using one-way ANOVA with Tukey’s HSD test. e The interaction of EGFR with EGF, CS-C, or CS-A was analyzed via SPR. f Similarly, the interaction of EGF with EGFR, CS-C, or CS-A was analyzed by SPR.