Insights from honeybee (Apis mellifera) and fly (Drosophila melanogaster) nicotinic acetylcholine receptors: From genes to behavioral functions

Dupuis, Julien; Louis, Thierry; Gauthier, M.; Raymond, Valérie

doi:10.1016/j.neubiorev.2012.04.003

Cited by 70 publications

(67 citation statements)

References 113 publications

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“…Although the biological implications of these observations are not clear, the length of the TM3-TM4 intracellular loop domain is associated with the levels of cell surface and intracellular assembled receptors in mammals and influences functional properties (Kracun et al 2008). Studies of divergent subunit functions have been hindered by the failure to obtain functional nAChR channels composed of divergent group subunits (Dupuis et al 2012;Jones et al 2009). Further studies are required to determine the pharmacological properties and functional roles of these subunits.…”

Section: Discussionmentioning

confidence: 99%

“…Recent genome projects have revealed the total numbers of nAChR subunits in several insect species, including Drosophila melanogaster, Anopheles gambiae, Apis mellifera, Bombyx mori, and Tribolium castaneum (Dupuis et al 2012;Jones et al 2005;Jones et al 2006;Jones & Sattelle 2007Millar 2003;Shao et al 2007;Tomizawa & Casida 2001). Insect nAChRs exhibit unique characteristics, which are different from those of vertebrates.…”

Section: Introductionmentioning

confidence: 99%

“…In addition, only one or two β subunits are present in insects, whereas four β subunits have been identified in mammals (Jones & Sattelle 2010). However, each insect nAChR subunit has transcriptional variants produced by either alternative splicing or RNA editing, which may contribute to diverse nAChRs in insect species (Dupuis et al 2012).…”

Section: Introductionmentioning

confidence: 99%

“…Although a number of invertebrate nAChR subunit nucleotide sequences have been determined, functional studies have been limited because of the inability to express physiologically functional invertebrate nAChRs using heterologous systems such as Xenopus laevis oocytes or cell lines (Dupuis et al 2012;Millar 1999). Although the Sgα1 subunit from the locust Schistocerca gregaria and Mpα1 and Mpα2 from the aphid Myzus persicae formed homopentameric channels when expressed in Xenopus laevis oocytes (Amar et al 1995;Marshall et al 1990;Sgard et al 1998).…”

Section: Introductionmentioning

confidence: 99%

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Five nicotinic acetylcholine receptor subunits from the Morotoge shrimp,Pandalopsis japonica: cloning, tissue distribution, and functional expression inXenopusoocytes

Kim

Yoon

Park

et al. 2015

Animal Cells and Systems

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The nicotinic acetylcholine receptor (nAChR) is a member of the ligand-gated ion channel (LGIC) family and is composed of five subunits arranged around a central pore. Expressed sequence tag screening and traditional cloning strategies revealed five full-length cDNAs encoding nAChR subunit homologs (Pajα3, Pajα10, Pajα11, Pajα12, and Pajβ1) in the Morotoge shrimp, Pandalopsis japonica. The nAChR subunits exhibited common structural characteristics, including a signal peptide sequence, a large N-terminal extracellular domain with conserved motifs for ligand binding (loops A-F), and a transmembrane (TM) domain with four hydrophobic TM motifs (TM1-TM4). Based on the conserved GEK motifs located just before TM2, all five nAChR subunits from P. japonica appear to be cation-selective ion channels. Among the five subunits, Pajα3 and Pajβ1 clustered together with insect core groups, whereas Pajα10, Pajα11, and Pajα12 were classified as a divergent group. Three distinct transcripts were identified in Pajα3, presumably due to alternative splicing between TM3 and TM4, which may be involved in channel formation with other subunits. All five nAChR subunits were expressed predominantly in neuronal tissues, including the brain, sinus gland/X-organ complex, thoracic ganglia, and abdominal ganglia, with no significant differences in subunit expression levels among the neuronal tissues. The five shrimp nAChR subunits could not be functionally expressed in Xenopus oocytes, but coexpression of Pajβ1 and rat α4 subunit (Rα4) formed functional channels responding to acetylcholine. Functional expression of vertebrate α subunit (Rα4) with invertebrate β1 subunit (Pajβ1) will expand our knowledge regarding the structural characteristics and molecular gating mechanism of invertebrate nAChRs.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Five nicotinic acetylcholine receptor subunits from the Morotoge shrimp,Pandalopsis japonica: cloning, tissue distribution, and functional expression inXenopusoocytes

Kim

Yoon

Park

et al. 2015

Animal Cells and Systems

View full text Add to dashboard Cite

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“…14,15) The vertebrate nAChRs possess up to five binding sites lying at the interface between an α-subunit and either another α-subunit in its homopentameric form or a different α or complementary β-subunit in its heteropentameric form. [16][17][18] A similar arrangement for the agonist binding site in the invertebrate nAChR is also postulated, although the exact subunit composition of functional insect nAChRs remains unknown. 19) Unlike verterbrate nAChRs, heterologous expression of genuine heteropentameric (α and β subunit combinations) insect nAChRs has not been successful, although heteropentameric receptors composed of mixed α subunits has been achieved.…”

Section: Invertebrate Nicotinic Acetylcholine Receptorsmentioning

confidence: 99%

The invertebrate pharmacology of insecticides acting at nicotinic acetylcholine receptors

et al. 2017

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The nicotinic acetylcholine receptor (nAChR) is a ligand-gated ion channel composed of 5 protein subunits arranged around a central cation selective pore. Several classes of natural and synthetic insecticides mediate their effect through interacting at nAChRs. This review examines the basic pharmacology of the neonicotinoids and related chemistry, with an emphasis on sapfeeding insects from the order Hemiptera, the principle pest target for such insecticides. Although the receptor subunit stoichiometry for endogenous invertebrate nAChRs is unknown, there is clear evidence for the existence of distinct neonicotinoid binding sites in native insect preparations, which reflects the predicted wide repertoire of nAChRs and differing pharmacology within this insecticide class. The spinosyns are principally used to control chewing pests such as Lepidoptera, whilst nereistoxin analogues are used on pests of rice and vegetables through contact and systemic action, the pharmacology of both these insecticides is unique and different to that of the neonicotinoids.

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Smarter neuronal signaling complexes from existing components: How regulatory modifications were acquired during animal evolution

Thomas

Hayashi

2013

BioEssays

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Neurons of organisms with complex and flexible behavior, especially humans, must precisely control protein localization and activity to support higher brain functions such as learning and memory. In contrast, simpler organisms generally have simpler individual neurons, less complex nervous systems and display more limited behaviors. Strikingly, however, many key neuronal proteins are conserved between organisms that have very different degrees of behavioral complexity. Here we discuss a possible mechanism by which conserved neuronal proteins acquired new attributes that were crucial in the evolution of complexity of nervous system structure and function. Specifically, we hypothesize that vertebrate-specific post-translational palmitoylation sites and PDZ-binding protein-protein interaction motifs act as gain-of-function mutations, increasing the regulatory potential of conserved proteins without affecting their core functions. We further hypothesize that the additional regulation of neurotransmitter receptors and other membrane proteins made possible by these sites and motifs is critical for the function of complex nervous systems.

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Insights from honeybee (Apis mellifera) and fly (Drosophila melanogaster) nicotinic acetylcholine receptors: From genes to behavioral functions

Cited by 70 publications

References 113 publications

Five nicotinic acetylcholine receptor subunits from the Morotoge shrimp,Pandalopsis japonica: cloning, tissue distribution, and functional expression inXenopusoocytes

Five nicotinic acetylcholine receptor subunits from the Morotoge shrimp,Pandalopsis japonica: cloning, tissue distribution, and functional expression inXenopusoocytes

The invertebrate pharmacology of insecticides acting at nicotinic acetylcholine receptors

Smarter neuronal signaling complexes from existing components: How regulatory modifications were acquired during animal evolution

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