Rectification of ATP-gated current of rat P2X2 and P2X7 receptors depends on the cytoplasmic N-terminus

Biochem Biophys Res Commun. 2023 Dec 25:688:149213. doi: 10.1016/j.bbrc.2023.149213. Epub 2023 Nov 7.

Abstract

The phenotypes of ATP-gated currents thought ionotropic P2X channels depend on the composition of the oligomeric receptor. We constructed chimeric P2X2/P2X7 receptors to study the effect of cytoplasmic domains on rectification of current flow through the open channel. We found that the identity of the N-terminus determines the pattern of rectification, with chimeric receptors containing the N-terminus of the P2X2 receptor displaying inward rectification, and chimeric receptors containing the N-terminus of the P2X7 receptor displaying slightly outward rectification. In contrast, rectification of current through chimeric receptors with swapped C-termini always mimicked the wild-type receptor. Thus, our findings suggest that the N-terminus of P2X receptors regulate ion flow through the channel pore and are responsible in part for determining current rectification.

Keywords: N-terminus; P2X2 receptor; P2X7 receptor; Rectification.

MeSH terms

  • Adenosine Triphosphate*
  • Animals
  • Cytoplasm
  • Cytosol
  • Rats
  • Receptors, Purinergic P2X2 / genetics
  • Receptors, Purinergic P2X7* / genetics

Substances

  • Receptors, Purinergic P2X7
  • Adenosine Triphosphate
  • Receptors, Purinergic P2X2