Fig. 5 | Nature Communications

Fig. 5

From: Mutation of a single residue promotes gating of vertebrate and invertebrate two-pore domain potassium channels

Fig. 5

Gradual activation of TREK1 and TASK2 by a series of TM2.6 mutations. a Response of different TREK1 TM2.6 mutants to rubidium/potassium ion substitution. Ratios of whole-cell currents recorded at −110 mV for [Rb+]o 98 mM and [K+]o 98 mM. b Gradual increase of TASK2 activation kinetics and response to pH challenge for different TM2.6 mutants. Normalized current traces recorded at +40 mV (left panel) and corresponding activation constants (Tau (ms), middle panel). Ratios of whole-cell current recorded at 0 mV with extracellular pH 9.4 and pH 7.4 (right panel). Currents were recorded 24 h after injection of cRNA at 1 ng/oocyte. Each data point represents one oocyte; center lines, medians; open circles, means; box limits, 25th and 75th percentiles; whiskers, standard deviation. ANOVA, Tukey’s multiple comparison test, *p < 0.05

Back to article page