Figure 5. Molecular basis for TRPM2 sensitivity to acidic pHo. (A) Schematic structure of TRPM2 and positions of substituted amino acid residues in the putative pore region of hTRPM2 (top). Alignment of the residues in the putative pore region of mTRPM2 and hTRPM2 (bottom). (B) Average current amplitude of WT TRPM2 and the mutants at pHo 7.4 and 6.0. TRPM2 currents were elicited by voltage ramps, and the outward currents at +100 mV were measured. E960Q and the triple mutant H958Q-E960Q-D964N were nonfunctional channels. *, P < 0.05.
Figure 5.

Molecular basis for TRPM2 sensitivity to acidic pHo. (A) Schematic structure of TRPM2 and positions of substituted amino acid residues in the putative pore region of hTRPM2 (top). Alignment of the residues in the putative pore region of mTRPM2 and hTRPM2 (bottom). (B) Average current amplitude of WT TRPM2 and the mutants at pHo 7.4 and 6.0. TRPM2 currents were elicited by voltage ramps, and the outward currents at +100 mV were measured. E960Q and the triple mutant H958Q-E960Q-D964N were nonfunctional channels. *, P < 0.05.

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