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pubmed-article:1919573pubmed:abstractTextALS and ARD proteins are thought to represent a ligand binding and a structural subunit, respectively, of Drosophila nicotinic acetylcholine receptors (nAChRs). Here, antibodies raised against fusion constructs encompassing specific regions of the ALS and ARD proteins were used to investigate a potential association of these two polypeptides. Both ALS and ARD antisera removed 20-30% of the high-affinity binding sites for the nicotinic antagonist 125I-alpha-bungarotoxin (125I-alpha-Btx) from detergent extracts of fly head membranes. Combinations of both types of antisera also precipitated the same fraction of alpha-Btx binding sites, a result suggesting that both polypeptides are components of the previously defined class I 125I-alpha-Btx binding sites in the Drosophila CNS. 125I-alpha-Btx binding to a MS2 polymerase-ALS fusion protein containing the predicted antagonist binding region showed that the ALS protein indeed constitutes the ligand binding subunit of a nicotinic receptor complex. These data are consistent with neuronal nAChRs in Drosophila containing at least two types of subunits, ligand binding and structural ones.lld:pubmed
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pubmed-article:1919573pubmed:pagination1556-62lld:pubmed
pubmed-article:1919573pubmed:dateRevised2010-6-4lld:pubmed
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pubmed-article:1919573pubmed:year1991lld:pubmed
pubmed-article:1919573pubmed:articleTitleNeuronal nicotinic acetylcholine receptors in Drosophila: antibodies against an alpha-like and a non-alpha-subunit recognize the same high-affinity alpha-bungarotoxin binding complex.lld:pubmed
pubmed-article:1919573pubmed:affiliationZMBH, Universität Heidelberg, F.R.G.lld:pubmed
pubmed-article:1919573pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:1919573pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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