Journal article

MUTATION OF AN ARGININE RESIDUE IN THE HUMAN GLYCINE RECEPTOR TRANSFORMS BETA-ALANINE AND TAURINE FROM AGONISTS INTO COMPETITIVE ANTAGONISTS

S RAJENDRA, JW LYNCH, KD PIERCE, CR FRENCH, PH BARRY, PR SCHOFIELD

NEURON | CELL PRESS | Published : 1995

Abstract

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 muta..

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