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The purinergic P2X7 receptor (P2X7R) is a member of the family of ligand-gated ion channels composed of seven subtypes, P2X1–7. These receptors possess three subunits assembled as homoor heterotrimers to make functional receptors (Nicke et al., 1998, 2005), which has been confirmed by atomic force microscopy (Barrera et al, 2005) and by crystallography (Kawate et al, 2009). The P2X7R shares an overall membrane topology with the other members of this family of receptors; it contains two putative pore forming transmembrane segments, a large cysteine-rich ligand-binding extracellular domain, and intracellularly located N and C termini (Surprenant et al, 1996). This subtype is structurally distinguished from other members of P2XRs by its long intracellular C-terminal tail with multiple protein and lipid interaction motifs, besides a cysteine-rich 18 – amino acid segment. From a pharmacological point of view, the P2X7R requires at least a 100-fold higher ATP concentration for activation compared to other P2XRs (North, 2002). Extracellular divalent cation reduction increases agonist potency (Hibell et al, 2001; Michel et al, 1999). Moreover, extracellular cations and chloride have important effects on the channel gating (Gudipaty et al., 2001; Li et al., 2003, 2008, 2010; Riedel et al., 2007b; Virginio et al., 1997). In this context, P2X7R activation can sustainably induce a wide range of different intracellular signaling responses (Dubyak, 2007; North, 2002).

Intracellular Signaling Pathways Integrating the Pore Associated with P2X7R Receptor with Other Large Pores