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Mutation of an arginine residue in the human glycine receptor transforms beta-alanine and taurine from agonists into competitive antagonists


Agonist binding to the inhibitory glycine receptor (GlyR) initiates the opening of a chloride-selective channel that modulates the neuronal membrane potential. Point mutations of the GlyR, substituting Arg-271 with either Leu or Gln, have been shown to underlie the inherited neurological disorder startle disease (hyperekplexia). We show that these substitutions result in the redistribution of GlyR single-channel conductances to lower conductance levels. Additionally, the binding of the glycinergic agonists beta-alanine and taurine to mutated GlyRs does not initiate a chloride current, but instead competitively antagonizes currents activated by glycine. These findings are consistent with mutations of Arg-271 resulting in the uncoupling of the agonist binding process from the channel activation mechanism of the receptor.

Type Journal
ISBN 0896-6273 (Print)
Authors Rajendra, S.;Lynch, J. W.;Pierce, K. D.;French, C. R.;Barry, P. H.;Schofield, P. R. :
Publisher Name NEURON
Published Date 1995-01-01 00:00:00
Published Volume 14
Published Issue 1
Published Pages 169-75
Status Published In-print