Linked Life Data

14749834

Source:http://linkedlifedata.com/resource/pubmed/id/14749834

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pubmed-article:14749834pubmed:abstractTextIonotropic 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.lld:pubmed
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pubmed-article:14749834pubmed:articleTitleSOL-1 is a CUB-domain protein required for GLR-1 glutamate receptor function in C. elegans.lld:pubmed
pubmed-article:14749834pubmed:affiliationDepartment of Biology, University of Utah, Salt Lake City, Utah 84112-0840, USA.lld:pubmed
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pubmed-article:14749834pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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