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To obtain folded recombinant protein, the Kv7.1 CT protein was always coexpressed and copurified with WT Ca M (14).

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Dose–response curves were constructed with increasing concentrations of Kv7.1 proximal CT and fixed concentrations of D-Ca M (100 n M) in the presence (100 µM free Ca D-Ca M fluorescence emission in the presence and absence of Kv7.1 CT proximal CT.

Representative experiment showing the D-Ca M fluorescence (100 n M D-Ca M) emission spectrum in the absence and presence of increasing concentration of Kv7.1 CT proximal CT (helices A and B; 0–60 μM Kv7.1 CT proximal CT).

We and others have shown that LQT mutations impairing Ca M binding to Kv7.1 proximal CT affect channel gating, folding, and trafficking (11, 14).

Overexpression of Ca M in CHO cells was found to robustly reduce currents of Kv7.2, Kv7.4, and Kv7.5 but not reduce those of Kv7.1 and Kv7.3 (21).

Kv7.1 α-subunits can interact with each of five KCNE β-subunits, displaying distinct current characteristics (2 genes lead to life-threatening cardiac arrhythmias, causing long-QT (LQT) or short-QT syndromes and atrial fibrillation (9, 10).

Similar to all Kv channels, the Kv7.1 structure features six transmembrane segments (S1–S6) containing a voltage-sensing module (S1–S4) and a pore domain (S5 and S6).

Phosphatidylinositol-4,5-bisphosphate (PIP regulates Kv7.1 channel function by increasing the coupling between the voltage sensor domain and the pore region, thereby stabilizing channel open conformation and leading to increased current amplitude, slower deactivation kinetics, and a negative shift in the voltage dependence of activation (29, 32, 33, 35, 36).

Recent studies identified clusters of basic residues in the Kv7.1 membrane domain, specifically at the S2–S3 and S4–S5 intracellular linkers and in prehelix A, to be involved in PIP, respectively) in the presence of increasing concentrations of WT Ca M.

Our results suggest that, after receptor-mediated PIP genes, which cause cardiac arrhythmias, such as the long-QT syndrome (LQT) and atrial fibrillation.

The proximal Kv7.1 C terminus (CT) binds calmodulin (Ca M) and phosphatidylinositol-4,5-bisphosphate (PIP and the calcified Ca M N lobe to a previously unidentified site in Kv7.1 helix B, also known to harbor an LQT mutation.

4, except that higher membrane voltages of up to 100 m V were applied for the mutants because of their depolarizing shift.


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