Fig. 4: Interactions between the cytosolic and transmembrane domain of AtSLAC1. | Nature Communications

Fig. 4: Interactions between the cytosolic and transmembrane domain of AtSLAC1.

From: Structure of the Arabidopsis guard cell anion channel SLAC1 suggests activation mechanism by phosphorylation

Fig. 4

a Interactions between the pore-forming transmembrane helices and the cytosolic plug formed by the N- and C-terminal tails. b Residues from the IH2–3 linker interacts with both the transmembrane segments and the cytosolic tails. IH2–3 is colored magenta. c Inward current densities for the alanine mutants which are involved in the interactions between the plug and the transmembrane helices, or between IH2–3 and its surroundings, measured at −100 mV, respectively, in the HEK293T cells. d Inward current densities for the alanine mutants in combination with S59A measured at −100 mV in the HEK293T cells. For all the constructs examined in c and d, independent experiments were repeated and the number of cells used (n) for each construct were indicated under the column. Significances were determined using one-way ANOVA with Dunnett’s multiple comparisons test. **P < 0.01, ***P < 0.001, ****P < 0.0001, ns = not significant for WT versus mutants in c, or S59A versus the double mutants in d. Data are represented as mean ± S.E.M.

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