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TRESK background potassium channel is not gated at the helix bundle crossing near the cytoplasmic end of the pore

Fig 3

TRESK channel is inhibited by MARK2 and PKA phosphorylation.

Mouse TRESK channels were expressed in HEK293T cells. Experiments were done on excised inside-out patches. TRESK currents were measured at +60 mV by switching the K+-free bath solution to a high K+ solution (solution changes are marked with bars above the graphs). Application of ATP and purified MARK2 (16 μg/ml) or separate application of ATP or MARK2 are marked by the bars above the recordings. A, Representative recording showing that application of MARK2 and 2 mM ATP leads to inhibition of TRESK current by phosphorylation. B, Representative recording showing that separate application of 2 mM ATP and MARK2 does not have an effect on TRESK current. C, Representative recording showing that application of PKA (30 U/ml) in the presence of 1 mM cAMP, 1 mM DTT and 2 mM ATP inhibits TRESK current by phosphorylating the channel. D, Representative recording showing that application of PKA (30 U/ml) in the presence of 1 mM cAMP, 1 mM DTT, but in the absence of ATP has no effect on TRESK current. E, The effects of ATP, MARK2 and ATP+MARK2 on TRESK current have been summarized as a scatter plot. The averages of each group are plotted as column graphs. Statistical significant differences between the groups (p<0.05, determined by Kruskal-Wallis test followed by multiple comparisons of mean ranks) are marked with asterisks. F, The effects of PKA and PKA+ATP on TRESK current have been summarized as a scatter plot. The averages of each group are plotted as column graphs. Statistical significant differences between the groups (p<0.05, determined by the Mann-Whitney U test) are marked with asterisks.

Fig 3

doi: https://doi.org/10.1371/journal.pone.0197622.g003