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Sequence of a functional invertebrate GABA(A) receptor subunit which can form a chimeric receptor with a vertebrate α subunit
Journal article   Peer reviewed

Sequence of a functional invertebrate GABA(A) receptor subunit which can form a chimeric receptor with a vertebrate α subunit

Robert J Harvey, E Vreugdenhil, S H Zaman, N S Bhandal, P N R Usherwood, E A Barnard and M G Darlison
EMBO Journal, Vol.10(11), pp.3239-3245
1991
url
https://doi.org/10.1002/j.1460-2075.1991.tb04887.xView
Published Version

Abstract

chimeric receptor expression GABAA receptor invertebrate receptor Lymnaea stagnalis polymerase chain reaction
The sequence of an invertebrate GABA(A) receptor subunit is described. This was deduced from a cDNA which was isolated from the mollusc Lymnaea stagnalis and w hich corresponds to a transcript of extremely low abundance. The cDNA was isolated using short exonic sequences from part of the corresponding gene in combination ith a variant of the polymerase chain reaction (PCR) known as RACE rapid ampliflcation of cDNA ends) The mature polypeptide has a predicted molecular eight of 54 569 Daltons and exhibits ~ 50% identity to vertebrate GABA(A) receptor β subunits. The six intron-exon boundaries determined to date in the molluscan gene occur at the same relative positions as those found in vertebrate GABA(A) receptor genes. Functional expression, in Xenopus oocytes, of the molluscan cDNA alone results in the formation of GABA-activated chloride ion channels that have a finite open probability even in the absence of agonist. These GABA-evoked currents can be reversibly blocked by the vertebrate GABA(A) receptor antagonist bicuculline Surprisingly, the molluscan β subunit is capable of replacing vertebrate β subunits in co-expression experiments with the bovine GABA(A) receptor α1 subunit. These findings suggest that invertebrate GABA(A) receptors exist in vivo as hetero-oligomeric complexes.

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