Abstract
The acetylcholine receptor (AChR) mediates synaptic transmission on binding to the acetylcholine neurotransmitter. To gain further information on the composition and biosynthesis of this receptor (for review of properties see refs 1–3), we have extracted AChR mRNA and translated it in a cell-free system and also in Xenopus oocytes. The latter have been shown to be not only highly efficient translation systems for microinjected, heterologous mRNAs but they can also faithfully execute post-translational processes such as glycosylation, sequestration, pre-peptide cleavage and secretion of appropriate products4–7. As native AChR is found glycosylated and sequestered in the plasma membrane, this system is of potential interest in studying its biosynthesis. We report here that Xenopus oocytes efficiently assemble intact, multi-subunit AChR molecules which show properties characteristic of the native AChR, including the binding of α-bungarotoxin (α-BTX).
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Sumikawa, K., Houghton, M., Emtage, J. et al. Active multi-subunit ACh receptor assembled by translation of heterologous mRNA in Xenopus oocytes. Nature 292, 862–864 (1981). https://doi.org/10.1038/292862a0
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DOI: https://doi.org/10.1038/292862a0
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