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. 2017 Jun 29;8:43. doi: 10.1038/s41467-017-00061-1

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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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Fig. 8 — Molecular mechanisms of DFNB48/USH1J deafness. a Co-immunoprecipitation assays of differentially truncated N-terminal fragments of TMC1 and full-length CIB2 (top panels). Schematics of truncated N-terminal fragments of TMC1 are shown on the bottom left panel. Specific N-terminal domain of TMC1 (amino acids 81–130) is essential for binding to CIB2 (red dashed lines). b Top: The protein alteration identified in USH1J is shown in red, while the protein alterations identified in DFNB48 are shown in black. Bottom: Quantitative analysis of FRET efficiency in cells co-expressing EGFP tagged human TMC1 (donor) and V5 tagged human CIB2 with deafness causing mutations. Error bars represent SEM. Asterisks indicate statistical significance of FRET efficiency changes relative to the control interaction of TMC1 with wild-type CIB2 (ANOVA with Dunnett’s test)