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

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...

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Bibliographic Details
Published in:FEBS letters 1991-05, Vol.283 (1), p.73-77
Main Authors: Kuhse, J., Kuryatov, A., Maulet, Y., Malosio, M.L., Schmieden, V., Betz, H.
Format: Article
Language:English
Subjects:
Alternative splicing
Aminoacid receptors (glycine, glutamate, gaba)
Biological and medical sciences
Brain development
Cell receptors
Cell structures and functions
Fundamental and applied biological sciences. Psychology
Glycine receptor
Molecular and cellular biology
Receptor heterogeneity
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Summary: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.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(91)80557-J