Figure 6. A conserved triplet of basic residues in the helix A-B linker is critical for PIP2 interactions with Kv7.2, as shown by charge-reversal substitutions. Shown are single-channel records in the cell-attached (A) or inside-out patch (B) configurations of the indicated Kv7.2 wt or mutant channel at a membrane potential of 0 mV. The inside-out patches were perfused with diC8-PIP2 at 25 μM, which mostly closely corresponds to the activity seen in the cell-attached patch (see Results). The traces labeled KRR-EEE are from a triple mutant consisting of K452E/K459E/R461E. (C) Bars indicate the summarized Po values at 0 mV for the cell-attached (C-A) or inside-out patch (25 μM i-o) data for the indicated channel type. Asterisks above each bar indicate the level of significance compared with the corresponding values for wt Kv7.2. **, P < 0.01; ***, P < 0.001.
Figure 6.

A conserved triplet of basic residues in the helix A-B linker is critical for PIP2 interactions with Kv7.2, as shown by charge-reversal substitutions. Shown are single-channel records in the cell-attached (A) or inside-out patch (B) configurations of the indicated Kv7.2 wt or mutant channel at a membrane potential of 0 mV. The inside-out patches were perfused with diC8-PIP2 at 25 μM, which mostly closely corresponds to the activity seen in the cell-attached patch (see Results). The traces labeled KRR-EEE are from a triple mutant consisting of K452E/K459E/R461E. (C) Bars indicate the summarized Po values at 0 mV for the cell-attached (C-A) or inside-out patch (25 μM i-o) data for the indicated channel type. Asterisks above each bar indicate the level of significance compared with the corresponding values for wt Kv7.2. **, P < 0.01; ***, P < 0.001.

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