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Alternative splicing generates two isoforms of the α2 subunit of the inhibitory glycine receptor
Author(s) -
Kuhse J.,
Kuryatov A.,
Maulet Y.,
Malosio M.L.,
Schmieden V.,
Betz H.
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80557-j
Subject(s) - glycine receptor , alternative splicing , interleukin 10 receptor, alpha subunit , gene isoform , protein subunit , interleukin 5 receptor alpha subunit , g alpha subunit , biology , cys loop receptors , strychnine , scn3a , alpha (finance) , xenopus , microbiology and biotechnology , homomeric , heterologous expression , minigene , rna splicing , inhibitory postsynaptic potential , receptor , glycine , biochemistry , neuroscience , amino acid , gene , rna , recombinant dna , nicotinic agonist , nicotinic acetylcholine receptor , patient satisfaction , construct validity , medicine , nursing
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.