Source:http://linkedlifedata.com/resource/pubmed/id/14749834
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6973
|
pubmed:dateCreated |
2004-1-29
|
pubmed:abstractText |
Ionotropic glutamate receptors (iGluRs) mediate most excitatory synaptic signalling between neurons. Binding of the neurotransmitter glutamate causes a conformational change in these receptors that gates open a transmembrane pore through which ions can pass. The gating of iGluRs is crucially dependent on a conserved amino acid that was first identified in the 'lurcher' ataxic mouse. Through a screen for modifiers of iGluR function in a transgenic strain of Caenorhabditis elegans expressing a GLR-1 subunit containing the lurcher mutation, we identify suppressor of lurcher (sol-1). This gene encodes a transmembrane protein that is predicted to contain four extracellular beta-barrel-forming domains known as CUB domains. SOL-1 and GLR-1 are colocalized at the cell surface and can be co-immunoprecipitated. By recording from neurons expressing GLR-1, we show that SOL-1 is an accessory protein that is selectively required for glutamate-gated currents. We propose that SOL-1 participates in the gating of non-NMDA (N-methyl-D-aspartate) iGluRs, thereby providing a previously unknown mechanism of regulation for this important class of neurotransmitter receptor.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Caenorhabditis elegans Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Glutamic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, AMPA,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Glutamate,
http://linkedlifedata.com/resource/pubmed/chemical/glr-1 protein, C elegans
|
pubmed:status |
MEDLINE
|
pubmed:month |
Jan
|
pubmed:issn |
1476-4687
|
pubmed:author | |
pubmed:issnType |
Electronic
|
pubmed:day |
29
|
pubmed:volume |
427
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
451-7
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:14749834-Amino Acid Sequence,
pubmed-meshheading:14749834-Animals,
pubmed-meshheading:14749834-Biological Transport,
pubmed-meshheading:14749834-Caenorhabditis elegans,
pubmed-meshheading:14749834-Caenorhabditis elegans Proteins,
pubmed-meshheading:14749834-Cells, Cultured,
pubmed-meshheading:14749834-Electric Conductivity,
pubmed-meshheading:14749834-Glutamic Acid,
pubmed-meshheading:14749834-Molecular Sequence Data,
pubmed-meshheading:14749834-Neurons,
pubmed-meshheading:14749834-Protein Structure, Tertiary,
pubmed-meshheading:14749834-Receptors, AMPA,
pubmed-meshheading:14749834-Receptors, Glutamate
|
pubmed:year |
2004
|
pubmed:articleTitle |
SOL-1 is a CUB-domain protein required for GLR-1 glutamate receptor function in C. elegans.
|
pubmed:affiliation |
Department of Biology, University of Utah, Salt Lake City, Utah 84112-0840, USA.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|