Source:http://linkedlifedata.com/resource/pubmed/id/21252855
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
2011-2-17
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pubmed:abstractText |
At Caenorhabditis elegans neuromuscular junctions (NMJs), synaptic clustering of the levamisole-sensitive acetylcholine receptors (L-AChRs) relies on an extracellular scaffold assembled in the synaptic cleft. It involves the secreted protein LEV-9 and the ectodomain of the transmembrane protein LEV-10, which are both expressed by muscle cells. L-AChRs, LEV-9 and LEV-10 are part of a physical complex, which localizes at NMJs, yet none of its components localizes independently at synapses. In a screen for mutants partially resistant to the cholinergic agonist levamisole, we identified oig-4, which encodes a small protein containing a single immunoglobulin domain. The OIG-4 protein is secreted by muscle cells and physically interacts with the L-AChR/LEV-9/LEV-10 complex. Removal of OIG-4 destabilizes the complex and causes a loss of L-AChR clusters at the synapse. Interestingly, OIG-4 partially localizes at NMJs independently of LEV-9 and LEV-10, thus providing a potential link between the L-AChR-associated scaffold and local synaptic cues. These results add a novel paradigm for the immunoglobulin super-family as OIG-4 is a secreted protein required for clustering ionotropic receptors independently of synapse formation.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Anthelmintics,
http://linkedlifedata.com/resource/pubmed/chemical/Caenorhabditis elegans Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cholinergic Agonists,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulins,
http://linkedlifedata.com/resource/pubmed/chemical/Levamisole,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cholinergic
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
1460-2075
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:day |
16
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pubmed:volume |
30
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
706-18
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pubmed:meshHeading |
pubmed-meshheading:21252855-Animals,
pubmed-meshheading:21252855-Animals, Genetically Modified,
pubmed-meshheading:21252855-Anthelmintics,
pubmed-meshheading:21252855-Caenorhabditis elegans,
pubmed-meshheading:21252855-Caenorhabditis elegans Proteins,
pubmed-meshheading:21252855-Cholinergic Agonists,
pubmed-meshheading:21252855-Drug Resistance,
pubmed-meshheading:21252855-Immunoglobulins,
pubmed-meshheading:21252855-Levamisole,
pubmed-meshheading:21252855-Models, Biological,
pubmed-meshheading:21252855-Neuromuscular Junction,
pubmed-meshheading:21252855-Protein Binding,
pubmed-meshheading:21252855-Protein Structure, Tertiary,
pubmed-meshheading:21252855-Protein Transport,
pubmed-meshheading:21252855-Receptors, Cholinergic,
pubmed-meshheading:21252855-Tissue Distribution
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pubmed:year |
2011
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pubmed:articleTitle |
A single immunoglobulin-domain protein required for clustering acetylcholine receptors in C. elegans.
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pubmed:affiliation |
Biology Department, Ecole Normale Supérieure, IBENS, Paris, France.
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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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