Characterization of the subunit composition and structure of adult human glycine receptors

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16 Scopus citations


The strychnine-sensitive pentameric glycine receptor (GlyR) mediates fast inhibitory neurotransmission in the mammalian nervous system. Only heteromeric GlyRs mediate synaptic transmission, as they contain the β subunit that permits clustering at the synapse through its interaction with scaffolding proteins. Here, we show that α2 and β subunits assemble with an unexpected 4:1 stoichiometry to produce GlyR with native electrophysiological properties. We determined structures in multiple functional states at 3.6–3.8 Å resolutions and show how 4:1 stoichiometry is consistent with the structural features of α2β GlyR. Furthermore, we show that one single β subunit in each GlyR gives rise to the characteristic electrophysiological properties of heteromeric GlyR, while more β subunits render GlyR non-conductive. A single β subunit ensures a univalent GlyR-scaffold linkage, which means the scaffold alone regulates the cluster properties.

Original languageEnglish (US)
Pages (from-to)2707-2716.e6
Issue number17
StatePublished - Sep 1 2021


  • cryo-EM structure
  • heteromeric glycine receptor
  • planar bilayer recording
  • stepwise photobleaching
  • stoichiometry

ASJC Scopus subject areas

  • Neuroscience(all)


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