Coexpression of P2X2 and P2X3 receptor subunits can account for ATP-gated currents in sensory neurons

Nature. 1995 Oct 5;377(6548):432-5. doi: 10.1038/377432a0.


Cation-selective P2X receptor channels were first described in sensory neurons where they are important for primary afferent neurotransmission and nociception. Here we report the cloning of a complementary DNA (P2X3) from rat dorsal root ganglia that had properties dissimilar to those of sensory neurons. We also found RNA for (P2X1)(ref. 7), (P2X2)(ref. 8) and P2X4 (ref. 9) in sensory neurons; channels expressed from individual cDNAs did not reproduce those of sensory ganglia. Coexpression of P2X3 with P2X2, but not other combinations, yielded ATP-activated currents that closely resembled those in sensory neurons. These properties could not be accounted for by addition of the two sets of channels, indicating that a new channel had formed by subunit heteropolymerization. Although in some tissues responses to ATP can be accounted for by homomeric channels, our results indicate that ATP-gated channels of sensory neurons may form by a specific heteropolymerization of P2X receptor subunits.

MeSH terms

  • Adenosine Triphosphate / metabolism*
  • Amino Acid Sequence
  • Animals
  • Cell Line
  • Cloning, Molecular
  • DNA, Complementary
  • Ganglia, Spinal / metabolism
  • Ion Channel Gating*
  • Molecular Sequence Data
  • Neurons, Afferent / metabolism*
  • Rats
  • Receptors, Purinergic P2 / biosynthesis
  • Receptors, Purinergic P2 / metabolism*
  • Receptors, Purinergic P2X2
  • Receptors, Purinergic P2X3
  • Sequence Homology, Amino Acid
  • Transfection


  • DNA, Complementary
  • P2rx2 protein, rat
  • P2rx3 protein, rat
  • Receptors, Purinergic P2
  • Receptors, Purinergic P2X2
  • Receptors, Purinergic P2X3
  • Adenosine Triphosphate

Associated data

  • GENBANK/X91167