Assembly of the inhibitory glycine receptor: identification of amino acid sequence motifs governing subunit stoichiometry

Neuron. 1993 Dec;11(6):1049-56. doi: 10.1016/0896-6273(93)90218-g.


The inhibitory glycine receptor (GlyR) is a pentameric protein composed of two types (alpha and beta) of membrane-spanning subunits. Coexpression in Xenopus oocytes of a low affinity mutant of the alpha 2 subunit with the alpha 1 and beta subunits indicated that GlyRs assembled from alpha 1 and alpha 2 polypeptides contain variable subunit ratios, whereas alpha/beta hetero-oligomers have an invariant (3:2) stoichiometry. Analysis of different alpha/beta chimeric constructs revealed that this difference in assembly behavior is mediated by the N-terminal extracellular regions of the receptor subunits. Substitution of residues diverging between the alpha and beta subunits identified combinations of sequence motifs determining subunit stoichiometry.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • DNA Primers
  • Female
  • Humans
  • Kinetics
  • Macromolecular Substances
  • Membrane Potentials / physiology
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed
  • Oocytes / physiology
  • Polymerase Chain Reaction
  • RNA, Complementary / metabolism
  • Rats
  • Receptors, Glycine / biosynthesis*
  • Receptors, Glycine / metabolism
  • Receptors, Glycine / physiology
  • Recombinant Fusion Proteins / biosynthesis
  • Recombinant Fusion Proteins / metabolism
  • Xenopus


  • DNA Primers
  • Macromolecular Substances
  • RNA, Complementary
  • Receptors, Glycine
  • Recombinant Fusion Proteins