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. 2019 Jul 24;2:270. doi: 10.1038/s42003-019-0503-6

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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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Fig. 5 — Localisation of the SLC26A7 p.Gln500Ter mutant. a Immunoblotting to confirm the FLAG-tagged SLC26A7 mutant in MDCK cells. β-actin served as an internal control; dox, doxycycline. Arrowheads indicate glycosylated wild type SLC26A7 (1), glycosylated SLC26A7 p.Gln500ter mutant (2), wild-type SLC26A7 (3), and SLC26A7 p.Gln500ter mutant (4). b Immunofluorescence analysis for FLAG (red) FLAG-tagged SLC26A7 mutant-transfected MDCK cells. Propidium iodide (blue) marks cell nuclei. c SLC26A7 protein structure and the positions of mutations in patients with congenital hypothyroidism. The SLC26A7 protein has 12 putative transmembrane and intracellular N- and C-terminal domains. The C-terminal cytoplasmic domain contains the STAS domain, which is shared among SLC26 family members. The mutations identified in our patients (filled star) and in the previously reported Arabian patients (open star) are illustrated. TM, transmembrane domain; STAS, sulphate transporters and anti-sigma factor antagonists