M2 pore mutations convert the glycine receptor channel from being anion- to cation-selective

Citations of this article
Mendeley users who have this article in their library.


Three mutations in the M2 transmembrane domains of the chloride- conducting α1 homomeric glycine receptor (P250Δ, A251E, and T265V), which normally mediate fast inhibitory neurotransmission, produced a cation- selective channel with P(Cl)/P(Na), = 0.27 (wild-type P(Cl)/P(Na) = 25), a permeability sequence P(Cs) > P(K) > P(Na) > P(Li), an impermeability to Ca 2+ , and a reduced glycine sensitivity. Outside-out patch measurements indicated reversed and accentuated rectification with extremely low mean single channel conductances of 3 pS (inward current) and 11 pS (outward current). The three inverse mutations, to those analyzed in this study, have previously been shown to make the α7 acetylcholine receptor channel anion- selective, indicating a common location for determinants of charge selectivity of inhibitory and excitatory ligand-gated ion channels.




Keramidas, A., Moorhouse, A. J., French, C. R., Schofield, P. R., & Barry, P. H. (2000). M2 pore mutations convert the glycine receptor channel from being anion- to cation-selective. Biophysical Journal, 79(1), 247–259. https://doi.org/10.1016/S0006-3495(00)76287-4

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free