Fig. 1
Biophysical properties of Kv1.3 channels following mutations of the acidic ER export motif. a Bar graph of the mean peak (left) or sustained (middle) current (± s.e.m.) for various voltage-clamped Kv1.3-eGFP or mutant channels as recorded in cell-attached patches using a single step depolarization of +40 mV (Vc) from a holding potential (Vh) of -80 mV. Representative current traces comparing Kv1.3-eGFP with that of Kv1.3-eGFP ∆C (right). b Same as in (A) but comparing inactivation (left) or deactivation (middle) kinetics of Kv1.3-eGFP. Significantly different by one-way ANOVA, Bonferoni’s post-hoc test, * = 0.001. c Line graph of the normalized tail currents is fit with a Boltzmann relation to calculate voltage at half-activation (V1/2). Significantly different V1/2 by one-way ANOVA, Bonferoni’s post-hoc test, *** = 0.0001, * = 0.001