LIN-23-mediated degradation of beta-catenin regulates the abundance of GLR-1 glutamate receptors in the ventral nerve cord of C. elegans

Neuron. 2005 Apr 7;46(1):51-64. doi: 10.1016/j.neuron.2004.12.058.

Abstract

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.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Blotting, Western
  • Caenorhabditis elegans
  • Caenorhabditis elegans Proteins / genetics
  • Caenorhabditis elegans Proteins / metabolism*
  • Cell Cycle Proteins / genetics
  • Cell Cycle Proteins / metabolism*
  • Central Nervous System / physiology*
  • Cytoskeletal Proteins / metabolism*
  • F-Box Proteins / genetics
  • F-Box Proteins / metabolism*
  • Mutation
  • Neurons / metabolism
  • Polymerase Chain Reaction
  • Receptors, AMPA / metabolism*
  • Trans-Activators / metabolism*
  • Transgenes
  • beta Catenin

Substances

  • Caenorhabditis elegans Proteins
  • Cell Cycle Proteins
  • Cytoskeletal Proteins
  • F-Box Proteins
  • Receptors, AMPA
  • Trans-Activators
  • beta Catenin
  • glr-1 protein, C elegans
  • lin-23 protein, C elegans