Abstract
P2X receptors are ligand-gated ion channels that, when exposed to extracellular ATP, open a transmembrane channel that is non-selectively permeable for cations. Seven isoforms are known, P2X1-P2X7. Like all P2X subunits (except P2X6), P2X7 subunits assemble as homotrimeric complexes. While other P2X subunits also efficiently form heterotrimeric P2X receptors, heterotrimer formation involving the P2X7 subunit is suggested only for the P2X4 subunit. Here, we performed co-purification experiments with the P2X7 subunit co-expressed with P2X1 or P2X4 subunits in X.
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