Biochemical and functional evidence for heteromeric assembly of P2X1 and P2X4 subunits.

@article{Nicke2005BiochemicalAF,
  title={Biochemical and functional evidence for heteromeric assembly of P2X1 and P2X4 subunits.},
  author={Annette Nicke and Daniel Kerschensteiner and Florentina Soto},
  journal={Journal of neurochemistry},
  year={2005},
  volume={92 4},
  pages={925-33}
}
P2X receptors are ligand-gated ion channels activated by extracellular ATP. In expression systems, P2X subunits form homo- and heterotrimeric receptors. Heteromerization is also likely to occur in vivo as (i) most P2X subunits show overlapping distribution in different tissues and (ii) the functional properties of many native P2X receptors differ from those of heterologously expressed homomeric receptors. Here, we used the Xenopus laevis oocyte expression system to test for heteromerization of… CONTINUE READING
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