Abstract
LIGAND-gated ion channels, a major class of cell-surface proteins, have a pseudosymmetric structure with five highly homologous subunits arranged around a central ion pore1. The correct assembly of each channel, whose subunit composition varies with cell type and stage of development, requires specific recognition between the subunits2–4. Assembly of the pentameric form of the acetylcholine receptor from adult muscle (AChR; α2βɛδ) proceeds by a stepwise pathway starting with the formation of the hetero-dimers, αe and α δ. The heterodimers then associate with the β subunit and with each other to form the complete receptor5–7,21. We have now determined which parts of the subunits mediate the interactions during assembly of the adult form of the receptor from mouse muscle by using a chimaeric subunit in which the N-terminal and C-terminal extracellular domains are derived from the ɛ subunit with the remainder from the β subunit. The e and β subunits were chosen because the subunit forms a heterodimer with the a subunit in the pathway for assembly of the receptor,whereas the β subunit does not. The ɛβ chimaera can substitute for the ɛ but not the β subunit in the oligomeric receptor, indicating that the a subunit specifically recognizes an extracellular domain of the e subunit.
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Yu, XM., Hall, Z. Extracellular domains mediating ɛ subunit interactions of muscle acetylcholine receptor. Nature 352, 64–67 (1991). https://doi.org/10.1038/352064a0
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DOI: https://doi.org/10.1038/352064a0
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