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CKII and Ank-3 regulate ENaC activity
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Description
We hypothesize 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.
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