SOL-1 is an auxiliary subunit that modulates the gating of GLR-1 glutamate receptors in Caenorhabditis elegans.
Most rapid excitatory synaptic signaling in the brain is mediated by postsynaptic ionotropic glutamate receptors (iGluRs) that are gated open by the neurotransmitter glutamate. In Caenorhabditis elegans, sol-1 encodes a CUB-domain transmembrane protein that is required for currents that are mediated by the GLR-1 iGluR. Mutations in sol-1 do not affect GLR-1 expression, localization, membrane insertion, or stabilization at synapses, suggesting that SOL-1 is required for iGluR function. Here, we provide evidence that SOL-1 is an auxiliary subunit that modulates the gating of GLR-1 receptors. We show that mutant variants of GLR-1 with altered gating partially restore glutamate-gated current and GLR-1-dependent behaviors in sol-1 mutants. Domain analysis of SOL-1 indicates that extracellular CUB domain 3 is required for function and that a secreted variant partially restores glutamate-gated currents and behavior. Also, we show that endogenous glutamatergic synaptic currents are absent in sol-1 mutants. Our data suggest that GLR-1 iGluRs are not simply stand-alone molecules and require the SOL-1 auxiliary protein to promote the open state of the receptor. Our analysis presents the possibility that glutamatergic signaling in other organisms may be similarly modified by SOL-1-like transmembrane proteins.
Zheng
Yi
Y
Department of Biology, University of Utah, Salt Lake City, UT 84112-0840, USA.
Brockie
Penelope J
PJ
Mellem
Jerry E
JE
Madsen
David M
DM
Walker
Craig S
CS
Francis
Michael M
MM
Maricq
Andres V
AV
D000818:Animals; D001522:Behavior, Animal; D017173:Caenorhabditis elegans; D029742:Caenorhabditis elegans Proteins / Q000502:physiology*; D002462:Cell Membrane / Q000378:metabolism; D004594:Electrophysiology; D014644:Genetic Variation; D018698:Glutamic Acid / Q000737:chemistry; D049452:Green Fluorescent Proteins / Q000378:metabolism; D047468:Immunoprecipitation; D007700:Kinetics; D008024:Ligands; D008565:Membrane Proteins / Q000737:chemistry; D008957:Models, Genetic; D009154:Mutation; D009865:Oocytes / Q000378:metabolism; D010957:Plasmids / Q000378:metabolism; D017434:Protein Structure, Tertiary; D018091:Receptors, AMPA / Q000502:physiology*; D017470:Receptors, Glutamate / Q000378:metabolism; D015398:Signal Transduction; D009435:Synaptic Transmission; D013997:Time Factors; D014981:Xenopus
D029742:Caenorhabditis elegans Proteins; D008024:Ligands; D008565:Membrane Proteins; D018091:Receptors, AMPA; D017470:Receptors, Glutamate; C481340:SOL-1 protein, C elegans; C096470:glr-1 protein, C elegans; D049452:Green Fluorescent Proteins; D018698:Glutamic Acid