1471-4159/asset/cover.gif?v=1&s=4f99ec10d4bac18b4327882ae87f581a11d8dd49 "Journal of Neurochemistry")
The present address of Dr. H. Betz is Max-Planck-lnstitut für Hirnforschung, Deutschordenstrasse 46, D-6000 Frankfurt, F.R.G.
1471-4159/asset/olbannerleft.gif?v=1&s=4636ca86ad7e40d133e71d09a5d759010472e0c2)
1471-4159/asset/olbannerright.gif?v=1&s=38094197c2d87aeb3b86aa293b5858c5c15cca29)
Neuronal Nicotinic Acetylcholine Receptors in Drosophila: Antibodies Against an α-Like and a Non-α-Subunit Recognize the Same High-Affinity α-Bungarotoxin Binding Complex
Article first published online: 5 OCT 2006
DOI: 10.1111/j.1471-4159.1991.tb06351.x
Additional Information
How to Cite
Schloss, P., Betz, H., Schroder, C. and Gundelfinger, E. D. (1991), Neuronal Nicotinic Acetylcholine Receptors in Drosophila: Antibodies Against an α-Like and a Non-α-Subunit Recognize the Same High-Affinity α-Bungarotoxin Binding Complex. Journal of Neurochemistry, 57: 1556–1562. doi: 10.1111/j.1471-4159.1991.tb06351.x
- †
The present address of Dr. H. Betz is Max-Planck-lnstitut für Hirnforschung, Deutschordenstrasse 46, D-6000 Frankfurt, F.R.G.
Publication History
- Issue published online: 5 OCT 2006
- Article first published online: 5 OCT 2006
- Abstract
- Article
- References
- Cited By
Keywords:
- Neuronal nicotinic acetylcholine receptors;
- Immunoprecipitation;
- α-Bungarotoxin;
- Drosophila melanogaster.
Abstract
: ALS 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-α-bungarotoxin (125I-α-Btx) from detergent extracts of fly head membranes. Combinations of both types of antisera also precipitated the same fraction of α-Btx binding sites, a result suggesting that both polypeptides are components of the previously defined class I 125I-α-Btx binding sites in the Drosophila CNS. 125I-α-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.