%0 Journal Article
%T The Drosophila nicotinic acetylcholine receptor subunits D¦Á5 and D¦Á7 form functional homomeric and heteromeric ion channels
%A Stuart J Lansdell
%A Toby Collins
%A Jim Goodchild
%A Neil S Millar
%J BMC Neuroscience
%D 2012
%I BioMed Central
%R 10.1186/1471-2202-13-73
%X A full-length cDNA clone encoding the Drosophila nAChR D¦Á5 subunit has been isolated and the properties of D¦Á5-, D¦Á6- and D¦Á7-containing nAChRs examined in a variety of cell expression systems. We have demonstrated the functional expression, as homomeric nAChRs, of the D¦Á5 and D¦Á7 subunits in Xenopus oocytes by their co-expression with the molecular chaperone RIC-3. Also, using a similar approach, we have demonstrated the functional expression of a heteromeric ¡®triplet¡¯ nAChR (D¦Á5£¿+£¿D¦Á6£¿+£¿D¦Á7) with substantially higher apparent affinity for acetylcholine than is seen with other subunit combinations. In addition, specific cell-surface binding of [125I]-¦Á-bungarotoxin was detected in both Drosophila and mammalian cell lines when D¦Á5 was co-expressed with D¦Á6 and RIC-3. In contrast, co-expression of additional subunits (including D¦Á7) with D¦Á5 and D¦Á6 prevented specific binding of [125I]-¦Á-bungarotoxin in cell lines, suggesting that co-assembly with other nAChR subunits can block maturation of correctly folded nAChRs in some cellular environments.Data are presented demonstrating the ability of the Drosophila D¦Á5 and D¦Á7 subunits to generate functional homomeric and also heteromeric nAChRs.
%U http://www.biomedcentral.com/1471-2202/13/73/abstract