| http://purl.uniprot.org/citations/17314321 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/17314321 | http://www.w3.org/2000/01/rdf-schema#comment | "Nicotinic acetylcholine receptors (nAChRs) are pentameric neurotransmitter-gated ion channels that mediate synaptic transmission throughout the nervous system in vertebrates and invertebrates. Caenorhabditis elegans is a nonmammalian model for the study of the nervous system and a model of parasitic nematodes. Nematode muscle nAChRs are of considerable interest because they are targets for anthelmintic drugs. We show single-channel activity of C. elegans muscle nAChRs for the first time. Our results reveal that in the L1 larval stage acetylcholine (ACh) activates mainly a levamisole-sensitive nAChR (L-AChR). A single population of 39 pS channels, which are 5-fold more sensitive to levamisole than ACh, is detected. In contrast to mammalian nAChRs, open durations are longer for levamisole than for ACh. Studies in mutant strains reveal that UNC-38, UNC-63, and UNC-29 subunits are assembled into a single L-AChR in the L1 stage and that these subunits are irreplaceable, suggesting that they are vital for receptor function throughout development. Recordings from a strain mutated in the LEV-1 subunit show a main population of channels with lower conductance (26 pS), prolonged open durations, and reduced sensitivity to levamisole. Thus, although LEV-1 is preferentially incorporated into native L-AChRs, receptors lacking this subunit can still function. No single-channel activity from levamisole-insensitive nAChRs is detected. Thus, during neuromuscular transmission in C. elegans, the majority of ACh-activated current flows through L-AChRs. This study contributes to the understanding of the molecular mechanisms underlying functional diversity of the nAChR family and offers an excellent strategy to test novel antiparasitic drugs."xsd:string |
| http://purl.uniprot.org/citations/17314321 | http://purl.org/dc/terms/identifier | "doi:10.1124/mol.106.033514"xsd:string |
| http://purl.uniprot.org/citations/17314321 | http://purl.uniprot.org/core/author | "Bouzat C."xsd:string |
| http://purl.uniprot.org/citations/17314321 | http://purl.uniprot.org/core/author | "Hernando G."xsd:string |
| http://purl.uniprot.org/citations/17314321 | http://purl.uniprot.org/core/author | "Rayes D."xsd:string |
| http://purl.uniprot.org/citations/17314321 | http://purl.uniprot.org/core/author | "Flamini M."xsd:string |
| http://purl.uniprot.org/citations/17314321 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |
| http://purl.uniprot.org/citations/17314321 | http://purl.uniprot.org/core/name | "Mol Pharmacol"xsd:string |
| http://purl.uniprot.org/citations/17314321 | http://purl.uniprot.org/core/pages | "1407-1415"xsd:string |
| http://purl.uniprot.org/citations/17314321 | http://purl.uniprot.org/core/title | "Activation of single nicotinic receptor channels from Caenorhabditis elegans muscle."xsd:string |
| http://purl.uniprot.org/citations/17314321 | http://purl.uniprot.org/core/volume | "71"xsd:string |
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