Analysis of the solubilized nicotinic acetylcholine receptor of <i>Drosophila melanogaster</i>

Jiménez, Fernando; Rudloff, Eberhard

doi:10.1016/0014-5793(80)80587-4

Cited by 6 publications

(3 citation statements)

References 23 publications

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“…membranes are rather controversial. Some authors have described the existence of a single binding component with Kd values ranging from 2 x 10-9 M to 1.6 x 10-10 M (Schmidt-Nielsen et al, 1977;Dudai, 1978;Jimenez and Rudloff, 1980) while others have suggested the existence of multiple binding sites (Bartels, 1984;Nagursky, 1985). Whether ca-Btx binding interferes with the physiological ACh response in Drosophila, as it does at the vertebrate motor endplate, is presently unclear.…”

Section: Discussionmentioning

confidence: 99%

Neuronal acetylcholine receptors in Drosophila: the ARD protein is a component of a high-affinity alpha-bungarotoxin binding complex.

Schloss¹,

Hermans-Borgmeyer²,

Betz³

et al. 1988

The EMBO Journal

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The ard gene of Drosophila melanogaster encodes a structural homologue of vertebrate nicotinic acetylcholine receptors (AChR) and is expressed exclusively in nervous tissue. To study the nature of the ARD protein, antibodies were raised against fusion constructs containing two regions of this polypeptide. One segment is putatively extracellular (amino acids 65‐212), the other domain is exposed to the cytoplasm (amino acids 305‐444). The ARD antisera obtained served to investigate the physical relationship between the ARD protein and alpha‐bungarotoxin (alpha‐Btx) binding sites occurring in Drosophila. Two different high‐affinity binding sites for [125I]alpha‐Btx, a highly potent antagonist of vertebrate muscle AChR, were detected in fly head membranes. Equilibrium binding and kinetic studies revealed Kd values of approximately 0.1 nM (site 1) and approximately 4 nM (site 2). The estimated maximal binding (Bmax) was approximately 240 and 1080 fmol/mg protein respectively. Both sites exhibited a nicotinic‐cholinergic pharmacology. Immunoprecipitation experiments with the ARD antisera indicated that the ARD protein is associated with the [125I]alpha‐Btx binding site 1 only. These data support the previously postulated hypothesis that the ARD protein is part of an alpha‐Btx binding neuronal AChR of Drosophila. Furthermore, they indicate heterogeneity in nicotinic‐cholinergic binding sites in the insect nervous system.

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Section: Discussionmentioning

confidence: 99%

Neuronal acetylcholine receptors in Drosophila: the ARD protein is a component of a high-affinity alpha-bungarotoxin binding complex.

Schloss¹,

Hermans-Borgmeyer²,

Betz³

et al. 1988

The EMBO Journal

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“…(iii) The Drosophila AChR protein shares a higher degree of homology with vertebrate neural than with muscular AChR subunits (Table I). The ARD protein may therefore be a polypeptide of the previously characterized cabungarotoxin binding component of the Drosophila central nervous system (Schmidt-Nielsen et al, 1977;Dudai, 1978;Jimenez and Rudloff, 1978). From protein-chemical data, the native insect AChR of 250 000-300 000 mol.…”

Section: Discussionmentioning

confidence: 99%

“…In conclusion, our data strongly suggest that the ARD protein is part of a nicotinic receptor phylogenetically more primitive than the vertebrate non-neuronal AChRs. Definitive proof of its association with the insect neuronal AChR species identified by ligand-binding studies (Schmidt-Nielsen et al, 1977;Dudai, 1978;Jimenez and Rudloff, 1978;Breer et al, 1985) will require the isolation of the ARD protein and/or the analysis of a previously described Drosophila AChR mutant .…”

Section: Discussionmentioning

confidence: 99%

Primary structure of a developmentally regulated nicotinic acetylcholine receptor protein from Drosophila

et al. 1986

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Acetylcholine is a major excitatory neurotransmitter in the central nervous system of insects. Using DNA probes of the Torpedo nicotinic acetylcholine receptor (AChR) we have isolated two overlapping cDNA clones encoding a putative neuronal AChR protein from the fruitfly, Drosophila melanogaster. The predicted mature protein consists of 497 amino acids, has a calculated mol. wt of 57 340 and shows extensive homology to known AChR subunits from different species along its entire amino acid sequence. Northern analysis revealed a hybridizing mRNA of 3.2 kb in late embryo and in pupae. Expression of the corresponding AChR gene thus characterizes periods of neuronal differentiation in Drosophila.

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Insecticide Compounds, Acting on the Acetylcholine Receptor of the Insect Nervous System

Richter¹,

Otto²,

Mengs³

1989

Chemistry of Plant Protection

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Analysis of the solubilized nicotinic acetylcholine receptor of Drosophila melanogaster

Cited by 6 publications

References 23 publications

Neuronal acetylcholine receptors in Drosophila: the ARD protein is a component of a high-affinity alpha-bungarotoxin binding complex.

Neuronal acetylcholine receptors in Drosophila: the ARD protein is a component of a high-affinity alpha-bungarotoxin binding complex.

Primary structure of a developmentally regulated nicotinic acetylcholine receptor protein from Drosophila

Insecticide Compounds, Acting on the Acetylcholine Receptor of the Insect Nervous System

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