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- W1970890190 abstract "GABAA receptors, important sites of drug action, are chloride channels composed of 5 subunits chosen from among 19 or more. Alternative splicing for α5, α6, and ρ1 subunits results in truncated proteins which appear to lack function. We report a similar, relatively common (about 20%) form of alternative splicing of the α4 subunit mRNA in mice and humans which, remarkably, creates a severely truncated message containing only the first two and last coding exons, with a frameshift in between. The only apparent translation product includes a short piece (39 amino acids) of the N-terminus right after the signal peptide. The splicing was developmentally and regionally regulated; the highest proportions of truncated α4 mRNA, about 40%, were observed in embryonic day 18 whole brain and adult cerebellum. The truncated mRNA, when coexpresssed in human embryonic kidney (HEK) 293 cells with the complete α4 subunit and β1 and γ2S subunits, reduced observed GABA currents without kinetic alterations. No such effect of truncated α4 was observed with α1 subunit-containing receptors. Thus, the truncated α4 N-terminus may play a post-translational regulatory role in intracellular folding/glycosylation/assembly of the α4 subunit." @default.
- W1970890190 created "2016-06-24" @default.
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- W1970890190 date "2002-09-01" @default.
- W1970890190 modified "2023-09-25" @default.
- W1970890190 title "Alternative splicing of the GABAA receptor α4 subunit creates a severely truncated mRNA" @default.
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- W1970890190 doi "https://doi.org/10.1016/s0361-9230(02)00816-x" @default.
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