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Significance Unlike many ion channels whose pore conductances remain relatively stable over time, it is thought that prolonged ATP applications to P2X receptors cause a striking increase over time in the permeability of large molecules, a process dubbed pore dilation. However, this mechanism remains poorly understood and highly controversial. Here, we use different methods spanning single-channel recordings, photochemistry, molecular biology, and computations to show that contrary to longstanding view, rapid activation by ATP allows the stable passage of large cations through the P2X pore. We further discover that spermidine, a large natural cation known to modulate other ion channels, is able to transit through many P2X receptors, including those thought to be nondilating. Our data thus reveal an unacknowledged P2X-mediated signaling.

On the permeation of large organic cations through the pore of ATP-gated P2X receptors