Alternative splicing generates two isoforms of the α2 subunit of the inhibitory glycine receptor

J. Kuhse, A. Kuryatov, Y. Maulet, M. L. Malosio, V. Schmieden, H. Betz

Research output: Contribution to journalArticlepeer-review


The inhibitory glycine receptor (GlyR) is a ligand-gated chloride channel protein which displays developmental heterogeneity in the mammalian central nervous system. Here we describe 2 novel cDNA variants of the rat GlyR α2 subunit and demonstrate that alternative splicing generates these 2 isoforms. The deduced protein sequences (α2A and α2B) exhibit 99% identity with the previously characterized human α2 subunit. In situ hybridization revealed expression of both α2A und α2B mRNAs in the prenatal rat brain, suggesting that these variant proteins may have a role in synaptogenesis. Heterologous expression in Xenopus oocytes showed that the more abundantly expressed α2A subunit forms strychnine-sensitive ion channels which resemble human α2 subunit GlyRs in their electrophysiological properties.

Original languageEnglish
Pages (from-to)73-77
Number of pages5
JournalFEBS Letters
Issue number1
Publication statusPublished - May 20 1991


  • Alternative splicing
  • Brain development
  • Glycine receptor
  • Receptor heterogeneity

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology
  • Cell Biology
  • Genetics
  • Structural Biology


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