Functional and molecular diversity of purinergic ion channel receptors

A. B. MacKenzie, A. Surprenant, R. A. North

Research output: Contribution to journalArticlepeer-review


P2X receptors are membrane ion channels gated by extracellular adenosine 5'-triphosphate (ATP); nucleotides also activate a family of seven transmembrane G protein-coupled receptors (P2Y). P2X receptors are widely expressed on mammalian cells, where they can be broadly differentiated into three groups. The first group is almost equally well activated by ATP and its analog αβmethyleneATP (αβmeATP), whereas a second group is not activated by αβmeATP. A third-group type of receptor (termed P2Z) is distinguished by the fact that the channel opening is followed by cell permeabilization and lysis if the agonist application is continued for more than a few seconds. Seven cDNAs have been cloned that encode P2X receptor subunits. When expressed individually in heterologous systems, P2X1 and P2X3 subunits form channels activated by ATP or αβmeATP; whereas P2X2, P2X4, and P2X5 form channels activated by ATP but not αβmeATP. P2X6 receptors do not express readily, and P2X7 receptors correspond closely in their properties to P2Z. Further phenotypes can be produced when two subunits are coexpressed, indicating heteromultimerization. This chapter compares the properties of the native P2X receptors with those of the cloned and expressed subunits.
Original languageEnglish
Pages (from-to)716-729
Number of pages13
JournalAnnals of the New York Academy of Sciences
Publication statusPublished - 1999


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