Open AccessConserved SOL-1 proteins regulate ionotropic glutamate receptor desensitization
Author(s) -
Colin Walker,
Michael M. Francis,
Penelope J. Brockie,
David M. Madsen,
Yi Zheng,
Andres V. Maricq
Publication year - 2006
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.0604520103
Subject(s) - ionotropic effect , neurotransmission , glutamate receptor , biology , microbiology and biotechnology , kainate receptor , glutamatergic , neuroscience , biochemistry , receptor , ampa receptor
The neurotransmitter glutamate mediates excitatory synaptic transmission by activating ionotropic glutamate receptors (iGluRs). InCaenorhabditis elegans , the GLR-1 receptor subunit is required for glutamate-gated current in a subset of interneurons that control avoidance behaviors. Current mediated by GLR-1-containing iGluRs depends on SOL-1, a transmembrane CUB-domain protein that immunoprecipitates with GLR-1. We have found that reconstitution of glutamate-gated current in heterologous cells depends on three proteins, STG-1 (aC. elegans stargazin-like protein), SOL-1, and GLR-1. Here, we use genetic and pharmacological perturbations along with rapid perfusion electrophysiological techniques to demonstrate that SOL-1 functions to slow the rate and limit the extent of receptor desensitization as well as to enhance the recovery from desensitization. We have also identified a SOL-1 homologue fromDrosophila and show thatDro SOL1 has a conserved function in promotingC. elegans glutamate-gated currents. SOL-1 homologues may play critical roles in regulating glutamatergic neurotransmission in more complex nervous systems.