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Generation of Two Forms of the γ‐Aminobutyric Acid A Receptor γ‐ 2 ‐Subunit in Mice by Alternative Splicing
Author(s) -
Kofuji Paulo,
Wang Jia Bei,
Moss Stephen J.,
Huganir Richard L.,
Burt David R.
Publication year - 1991
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1991.tb08209.x
Subject(s) - alternative splicing , protein subunit , gamma aminobutyric acid receptor subunit alpha 1 , biology , interleukin 10 receptor, alpha subunit , serine , phosphorylation , biochemistry , aminobutyric acid , gabbr1 , amino acid , transmembrane protein , cys loop receptors , rna splicing , receptor , microbiology and biotechnology , g alpha subunit , enzyme linked receptor , gene , exon , protease activated receptor 2 , nicotinic agonist , nicotinic acetylcholine receptor , rna
Abstract: γ‐Aminobutyric acid A (GABA A ) receptors are multisubunit ligand‐gated ion channels which mediate neuronal inhibition by GABA and are composed of at least four subunit types (α, β, γ, and δ). The γ 2 ‐subunit appears to be essential for benzodiazepine modulation of GABA A receptor function. In cloning murine γ 2 ‐subunits, we isolated cDNAs encoding forms of the subunit that differ by the insertion of eight amino acids, LLRMFSFK, in the major intracellular loop between proposed transmembrane domains M3 and M4. The two forms of the γ 2 ‐subunit are generated by alternative splicing, as demonstrated by cloning and partial sequencing of the corresponding gene. The eight‐amino‐acid insertion encodes a potential consensus serine phosphorylation site for protein kinase C. These results suggest a novel mechanism for the regulation of the GABA A receptor by protein phosphorylation.