Location of a delta-subunit region determining ion transport through the 
acetylcholine receptor channel

Imoto, K.; Methfessel, Christoph; Sakmann, Bert; Mishina, Masayoshi; Mori, Y.; Konno, T.; Fukuda, K.; Kurasaki, M.; Bujo, Hideaki; Fujita, Y.; Numa, Shosaku

doi:10.1038/324670a0

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Location of a delta-subunit region determining ion transport through the acetylcholine receptor channel

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Sakmann, Bert
Department of Cell Physiology, Max Planck Institute for Medical Research, Max Planck Society;

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Imoto, K., Methfessel, C., Sakmann, B., Mishina, M., Mori, Y., Konno, T., et al. (1986). Location of a delta-subunit region determining ion transport through the acetylcholine receptor channel. Nature, 324(6098), 670-674. doi:10.1038/324670a0.

Cite as: http://hdl.handle.net/21.11116/0000-0000-CCF1-A

Abstract

The combination of complementary DNA expression and single-channel current analysis provides a powerful tool for studying the structure-function relationship of the nicotinic acetylcholine receptor (AChR) (refs 1-5). We have previously shown that AChR channels consisting of subunits from different species, expressed in the surface membrane of Xenopus oocytes, can be used to relate functional properties to individual subunits. Here we report that, in extracellular solution of low divalent cation concentration, the bovine AChR channel has a smaller conductance than the Torpedo AChR channel. Replacement of the delta-subunit of the Torpedo AChR by the bovine delta-subunit makes the channel conductance similar to that of the bovine AChR channel. To locate the region in the delta-subunit responsible for this difference, we have constructed chimaeric delta-subunit cDNAs with different combinations of the Torpedo and bovine counterparts. The conductances of AChR channels containing chimaeric delta-subunits suggest that a region comprising the putative transmembrane segment M2 and the adjacent bend portion between segments M2 and M3 is involved in determining the rate of ion transport through the open channel.