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Biophysics of P2X receptors

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Abstract

The P2X receptor is the baby brother of the ligand-gated ion channel super-family. An understanding of its role in human physiology is still developing, and no one truly knows how it works to transport ions across the membrane. In this study, we review some aspects of P2X channel biophysics, concentrating on ion permeation and gating. P2X channels transport both small and large cations and anions across cell membranes in a manner that depends on both the subunit composition of the receptor and the experimental conditions. We describe the pore properties of wild-type receptors and use the altered phenotypes of mutant receptors to point the way towards a structural model of the pore.

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Notes

  1. From, “What is Biophysics”. Online educational resources of the Biophysical Society.

  2. This is not to say that all P2X5 receptors show anion permeability. Although Lys52 is positionally conserved, the Cl− permeabilities of most P2X5 orthologs are unknown.

  3. Ding and Sachs labelled the two open states “O 1 ” and “O 2 ”. We call them “O A ” and “O B ” in this review to distinguish them from the two conductance states that describe the normal (NMDG+ impermeable, O 1 state) and dilated (NMDG+ permeable, O 2 state) forms of the pore.

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Acknowledgements

We thank Baljit Khakh and Fred Sachs for some of data shown in the figures. The Egan Laboratory gratefully acknowledges the financial assistance of the National Institutes of Health (USA).

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  1. Department of Pharmacological and Physiological Science, Saint Louis University School of Medicine, 1402 S. Grand Boulevard, St. Louis, MO, 63104, USA

    Terrance M. Egan, Damien S. K. Samways & Zhiyuan Li

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  1. Terrance M. Egan
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Correspondence to Terrance M. Egan.

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Egan, T.M., Samways, D.S.K. & Li, Z. Biophysics of P2X receptors. Pflugers Arch - Eur J Physiol 452, 501–512 (2006). https://doi.org/10.1007/s00424-006-0078-1

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