SOL-1 is a CUB-domain protein required for GLR-1 glutamate receptor function in C. elegans

Yi Zheng, Jerry E. Mellem, Penelope J. Brockie, David M. Madsen and Andres V. Maricq ()
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Yi Zheng: University of Utah
Jerry E. Mellem: University of Utah
Penelope J. Brockie: University of Utah
David M. Madsen: University of Utah
Andres V. Maricq: University of Utah

Nature, 2004, vol. 427, issue 6973, 451-457

Abstract: Abstract 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 mouse1. 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 β-barrel-forming domains known as CUB domains2,3. 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.

Date: 2004
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DOI: 10.1038/nature02244

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