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

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.

journal_name

Nature

journal_title

Nature

authors

Imoto K,Methfessel C,Sakmann B,Mishina M,Mori Y,Konno T,Fukuda K,Kurasaki M,Bujo H,Fujita Y

doi

10.1038/324670a0

subject

Has Abstract,Author List Incomplete

pub_date

1986-12-18 00:00:00

pages

670-4

issue

6098

eissn

0028-0836

issn

1476-4687

journal_volume

324

pub_type

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