Source:http://linkedlifedata.com/resource/pubmed/id/18408712
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
7190
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| pubmed:dateCreated |
2008-4-24
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| pubmed:abstractText |
In insects, each olfactory sensory neuron expresses between one and three ligand-binding members of the olfactory receptor (OR) gene family, along with the highly conserved and broadly expressed Or83b co-receptor. The functional insect OR consists of a heteromeric complex of unknown stoichiometry but comprising at least one variable odorant-binding subunit and one constant Or83b family subunit. Insect ORs lack homology to G-protein-coupled chemosensory receptors in vertebrates and possess a distinct seven-transmembrane topology with the amino terminus located intracellularly. Here we provide evidence that heteromeric insect ORs comprise a new class of ligand-activated non-selective cation channels. Heterologous cells expressing silkmoth, fruitfly or mosquito heteromeric OR complexes showed extracellular Ca2+ influx and cation-non-selective ion conductance on stimulation with odorant. Odour-evoked OR currents are independent of known G-protein-coupled second messenger pathways. The fast response kinetics and OR-subunit-dependent K+ ion selectivity of the insect OR complex support the hypothesis that the complex between OR and Or83b itself confers channel activity. Direct evidence for odorant-gated channels was obtained by outside-out patch-clamp recording of Xenopus oocyte and HEK293T cell membranes expressing insect OR complexes. The ligand-gated ion channel formed by an insect OR complex seems to be the basis for a unique strategy that insects have acquired to respond to the olfactory environment.
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| pubmed:commentsCorrections | |
| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Heterotrimeric GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Subunits,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Odorant
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| pubmed:status |
MEDLINE
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| pubmed:month |
Apr
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| pubmed:issn |
1476-4687
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| pubmed:author | |
| pubmed:issnType |
Electronic
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| pubmed:day |
24
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| pubmed:volume |
452
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
1002-6
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| pubmed:dateRevised |
2009-11-19
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| pubmed:meshHeading |
pubmed-meshheading:18408712-Animals,
pubmed-meshheading:18408712-Bombyx,
pubmed-meshheading:18408712-Calcium,
pubmed-meshheading:18408712-Cell Line,
pubmed-meshheading:18408712-Culicidae,
pubmed-meshheading:18408712-Drosophila melanogaster,
pubmed-meshheading:18408712-Electric Conductivity,
pubmed-meshheading:18408712-HeLa Cells,
pubmed-meshheading:18408712-Heterotrimeric GTP-Binding Proteins,
pubmed-meshheading:18408712-Humans,
pubmed-meshheading:18408712-Insects,
pubmed-meshheading:18408712-Ion Channel Gating,
pubmed-meshheading:18408712-Kinetics,
pubmed-meshheading:18408712-Ligands,
pubmed-meshheading:18408712-Odors,
pubmed-meshheading:18408712-Oocytes,
pubmed-meshheading:18408712-Patch-Clamp Techniques,
pubmed-meshheading:18408712-Protein Subunits,
pubmed-meshheading:18408712-Receptors, Odorant,
pubmed-meshheading:18408712-Smell,
pubmed-meshheading:18408712-Xenopus laevis
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| pubmed:year |
2008
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| pubmed:articleTitle |
Insect olfactory receptors are heteromeric ligand-gated ion channels.
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| pubmed:affiliation |
Department of Integrated Biosciences, The University of Tokyo, Chiba 277-8562, Japan.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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