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. 2021 Jul 16;11:14600. doi: 10.1038/s41598-021-94118-3

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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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/.

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CKII increases ENaC activity by phosphorylating β-ENaC within its anchor motif to promote Ank-3 mediated trafficking to the membrane. Proposed mechanism by which CKII modifies ENaC activity. Our hypothesis is that phosphorylation by CKII of a key serine residue in a consensus CKII site contained within a canonical anchor motif within the COOH-terminal domain of β-ENaC is necessary and sufficient for the channel to bind Ank-3 with the latter being necessary for appropriate channel locale and activity, which is required for the physiological function of the channel and the appropriate fine-tuning of renal Na⁺ excretion. Created with BioRender.com.