Pannexin-1 (PANX1)

Pannexin-1 (PANX1) is a highly conserved, large-pore, membrane-spanning ion channel that forms homo-heptamers to mediate the release of ATP and other small anions and metabolites from the cytosol to the extracellular space[3][5][7][9]. PANX1 participates in diverse physiological processes, particularly purinergic signaling, by enabling extracellular ATP signaling, which can trigger downstream effects on immune cells, blood vessels, and neurons[3][7][9][10]. The channel structure includes four transmembrane helices per protomer, a complex pore gating mechanism regulated by caspase cleavage, post-translational modification (notably N255 glycosylation), and potential for drug inhibition by small molecules such as carbenoxolone[1][2][3][5]. PANX1 plays central roles in inflammation, immune response (including pyroptosis), vascular biology, and is implicated in several neurological, cardiovascular, and oncological diseases. Ongoing structural and functional studies highlight opportunities and challenges for therapeutic targeting, given its broad expression and essential roles in cellular homeostasis and disease pathogenesis[3][7][9][10].

Other names

Panx1Pannexin1

Channel blockade (e.g., carbenoxolone binds the channel and physically blocks ATP/ion release pathway); Allosteric inhibition of channel gating; Disruption of channel opening, often mimicking physiological regulatory mechanisms (such as caspase cleavage during apoptosis).