The present address of Dr. H. Betz is Max-Planck-lnstitut für Hirnforschung, Deutschordenstrasse 46, D-6000 Frankfurt, F.R.G.
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
Journal of Neurochemistry
Volume 57, Issue 5, pages 1556–1562, November 1991
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
- Issue published online: 5 OCT 2006
- Article first published online: 5 OCT 2006
- Neuronal nicotinic acetylcholine receptors;
- Drosophila melanogaster.
: 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.