LIN-23-mediated degradation of beta-catenin regulates the abundance of GLR-1 glutamate receptors in the ventral nerve cord of C. elegans.
Ubiquitin-mediated protein degradation has been proposed to play an important role in regulating synaptic transmission. Here we show that LIN-23, the substrate binding subunit of a Skp1/Cullin/F Box (SCF) ubiquitin ligase, regulates the abundance of the glutamate receptor GLR-1 in the ventral nerve cord of C. elegans. Mutants lacking lin-23 had an increased abundance of GLR-1 in the ventral cord. The increase of GLR-1 was not caused by changes in the ubiquitination of GLR-1. Instead, SCF(LIN-23) regulates GLR-1 through the beta-catenin homolog BAR-1 and the TCF/Lef transcription factor homolog POP-1. We hypothesize that LIN-23-mediated degradation of BAR-1 beta-catenin regulates the transcription of Wnt target genes, which in turn alter postsynaptic properties.
Dreier
Lars
L
Department of Molecular Biology, Massachusetts General Hospital, Harvard Medical School, Boston, Massachusetts 02114, USA.
Burbea
Michelle
M
Kaplan
Joshua M
JM
D000818:Animals; D015153:Blotting, Western; D017173:Caenorhabditis elegans; D029742:Caenorhabditis elegans Proteins / Q000235:genetics / Q000378:metabolism*; D018797:Cell Cycle Proteins / Q000235:genetics / Q000378:metabolism*; D002490:Central Nervous System / Q000502:physiology*; D003598:Cytoskeletal Proteins / Q000378:metabolism*; D044783:F-Box Proteins / Q000235:genetics / Q000378:metabolism*; D009154:Mutation; D009474:Neurons / Q000378:metabolism; D016133:Polymerase Chain Reaction; D018091:Receptors, AMPA / Q000378:metabolism*; D015534:Trans-Activators / Q000378:metabolism*; D019076:Transgenes; D051176:beta Catenin
D029742:Caenorhabditis elegans Proteins; D018797:Cell Cycle Proteins; D003598:Cytoskeletal Proteins; D044783:F-Box Proteins; D018091:Receptors, AMPA; D015534:Trans-Activators; D051176:beta Catenin; C096470:glr-1 protein, C elegans; C418507:lin-23 protein, C elegans