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A neuronal nicotinic acetylcholine receptor subunit (α7) is developmentally regulated and forms a homo-oligomeric channel blocked by α-BTX

Published inNeuron, vol. 5, no. 6, p. 847-856
Publication date1990
Abstract

cDNA and genomic clones encoding α7, a novel neuronal nicotinic acetylcholine receptor (nAChR) α subunit, were isolated and sequenced. The mature α7 protein (479 residues) has moderate homology with all other α and non-α nAChR subunits and probably assumes the same transmembrane topology. α7 transcripts transiently accumulate in the developing optic tectum between E5 and E16. They are present in both the deep and the superficial layers of E12 tectum. In Xenopus oocytes, the α7 protein assembles into a homo-oligomeric channel responding to acetylcholine and nicotine. The α7 channel desensitizes very rapidly, rectifies strongly above -20 mV, and is blocked by α-bungarotoxin. A bacterial fusion protein encompassing residues 124-239 of α7 binds labeled α-bungarotoxin. We conclude that α-bungarotoxin binding proteins in the vertebrate nervous system can function as nAChRs.

Citation (ISO format)
COUTURIER-GOEBEL, Sabine et al. A neuronal nicotinic acetylcholine receptor subunit (α7) is developmentally regulated and forms a homo-oligomeric channel blocked by α-BTX. In: Neuron, 1990, vol. 5, n° 6, p. 847–856. doi: 10.1016/0896-6273(90)90344-F
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