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. Author manuscript; available in PMC: 2010 Apr 1.
Published in final edited form as: Nat Struct Mol Biol. 2009 Sep 27;16(10):1080–1085. doi: 10.1038/nsmb.1679

Figure 1.

Figure 1

Membrane modification alters gating of voltage-activated ion channels and a voltage-activated phosphatase. G-V and Q-V relations obtained for native membranes are shown in black, while those after treatment with SMaseD are shown in red. (a) Ionic current traces and G-V relations for Kv2.1. (b) Gating current traces and Q-V relations for Ci-VSP. (c) G-V curves for Kv2.1 chimeras that contain individual paddle motifs from each of the four domains of rNav1.4. The holding voltage was −100mV for Nav DI and Nav DII, and −120mV for Nav DIII and NavDIV chimeras; test pulse duration was 300ms (500ms for Nav DIV); tail voltage was −60mV for Nav DI, −80mV for Nav DII, −110mV for Nav DIII and −100mV for Nav DIV. (d) G-V curves for chimeras where complete (S3–S4) or partial (S4) paddle motifs of Kv2.1 were replaced with homologous regions from KvAP. The holding voltage was −100mV, test pulse duration was 300ms, and tail voltage was −80mV. In all cases conductance was determined from normalized tail currents. For ionic currents, leak, background and capacitive currents were isolated and subtracted after blocking the Kv channels with agitoxin-2, while for gating currents, they were subtracted using a P/−4 protocol. n=3, error bars are s.e.m.