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ATP opens ionotropic P2X channels through a process that is poorly understood. We made an array of mutant rat P2X2 channels containing unique alanine substitutions in the transmembrane segments with the goal of identifying possible secondary structure and mapping gating domains in the pore. Alteration of channel function was measured as a change in ATP potency, 2'-3'-O-(4-benzoylbenzoyl)ATP (BzATP) efficacy, and deactivation kinetics. Four mutants (V45A, Y47A, V51A, and D349A) failed to respond to ATP. Seven (H33A, Q37A, I40A, L41A, Y43A, F44A, and I50A) of 22 mutations in the first transmembrane segment (TM1) produced channels with altered potencies, and two mutants (Y43A and F44A) were active in the absence of agonist. The pattern of hits was consistent with a helical secondary structure. In contrast, nine (I328A, P329A, N333A, L338A, T339A, S340A, G342A, G344A, and S345A) of 24 mutations in the second transmembrane segment (TM2) resulted in a change in potency, but no regular pattern of impact was apparent. Many of the same mutations that altered ATP potency also changed the relative efficacy of the partial agonist BzATP. Together, these data suggest that both TM1 and TM2 participate in the conformational changes that occur during receptor activation and help to define domains involved in conformational switching within or near the pore.

Gain and Loss of Channel Function by Alanine Substitutions in the Transmembrane Segments of the Rat ATP-Gated P2X2Receptor

Gain and Loss of Channel Function by Alanine Substitutions in the Transmembrane Segments of the Rat ATP-Gated P2X₂Receptor