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TWIK-related two-pore domain K + channel-2 (TREK-2) has voltageindependent activity and shows additional activation by acidic intracellular pH (pH i ) via neutralizing the E 332 in the cytoplasmic C terminal (Ct). We reported opposite regulations of TREK-2 by phosphatidylinositol 4,5-bisphosphate (PIP 2 ) via the alkaline K 330 and triple Arg residues (R 355-357 ); inhibition and activation, respectively. The G 334 between them appeared critical because its mutation (G 334 A) endowed hTREK-2 with tonic activity, similar to the mutation of the inhibitory K 330 (K 330 A). To further elucidate the role of putative bent conformation at G 334 , we compared the dual mutation forms, K 330 A/G 334 A and G 334 A/R 355-7 A, showing higher and lower basal activity, respectively. The results suggested that the tonic activity of G 334 A owes to a dominant influence from R 355-7 . Since there are additional triple Arg residues (R 377-9 ) distal to R 355-7 , we also examined the triple mutant (G 334 A/R 355-7 A/R 377-9 A) that showed tonic inhibition same with G 334 A/R 355-7 A. Despite the state of tonic inhibition, the activation by acidic pH i was preserved in both G 334 A/R 355-7 A and G 334 A/R 355-7 A/R 377-9 A, similar to the R 355-7 A. Also, the inhibitory effect of ATP could be commonly demonstrated under the activation by acidic pH i in R 355-7 A, G 334 A/R 355-7 A, and G 334 A/R 355-7 A/R 377-9 A. These results suggest that the putative bent conformation at G 334 is important to set the tug-of-war between K 330 and R 355-7 in the PIP 2 -dependent regulation of TREK-2.

the korean journal of physiology and pharmacology/korean journal of physiology and pharmacology

Dual regulatory effects of PI(4,5)P2 on TREK-2 K+ channel through antagonizing interaction between the alkaline residues (K330 and R355-357) in the cytosolic C-terminal helix