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. 2022 May 18;13:2747. doi: 10.1038/s41467-022-30407-3

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© The Author(s) 2022

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. 4 — a A NKCC1 dimer structure highlights coupling among the N-terminal phosphoregulatory segment, extreme C-terminal tail, and ICL1. b The interface between the transmembrane (dodger blue) and a swapped C-terminal (khaki) domains is observed only in the herein described form of NKCC1_iii/bumetanide dimer. Polar interactions are indicated as dashed lines. c Cl⁻ transport rates in insect cells of wildtype human NKCC1 and mutants designed to disrupt the transmembrane and C-terminal domain interface. Each circle represents one kinetic measurement of a single sample in a 96 well plate. Unpaired one-tailed Student’s t tests are used for statistical analyses (n = 6; data are presented as mean values ± SD).