The immunoglobulin super family protein RIG-3 prevents synaptic potentiation and regulates Wnt signaling

Neuron. 2011 Jul 14;71(1):103-16. doi: 10.1016/j.neuron.2011.05.034.

Abstract

Cell surface Ig superfamily proteins (IgSF) have been implicated in several aspects of neuron development and function. Here, we describe the function of a Caenorhabditis elegans IgSF protein, RIG-3. Mutants lacking RIG-3 have an exaggerated paralytic response to a cholinesterase inhibitor, aldicarb. Although RIG-3 is expressed in motor neurons, heightened drug responsiveness was caused by an aldicarb-induced increase in muscle ACR-16 acetylcholine receptor (AChR) abundance, and a corresponding potentiation of postsynaptic responses at neuromuscular junctions. Mutants lacking RIG-3 also had defects in the anteroposterior polarity of the ALM mechanosensory neurons. The effects of RIG-3 on synaptic transmission and ALM polarity were both mediated by changes in Wnt signaling, and in particular by inhibiting CAM-1, a Ror-type receptor tyrosine kinase that binds Wnt ligands. These results identify RIG-3 as a regulator of Wnt signaling, and suggest that RIG-3 has an anti-plasticity function that prevents activity-induced changes in postsynaptic receptor fields.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Aldicarb / pharmacology
  • Animals
  • Caenorhabditis elegans
  • Caenorhabditis elegans Proteins / antagonists & inhibitors
  • Caenorhabditis elegans Proteins / genetics
  • Caenorhabditis elegans Proteins / metabolism
  • Caenorhabditis elegans Proteins / physiology*
  • Cell Adhesion Molecules / genetics
  • Cell Adhesion Molecules / physiology*
  • Excitatory Postsynaptic Potentials / drug effects
  • Excitatory Postsynaptic Potentials / genetics
  • Excitatory Postsynaptic Potentials / physiology*
  • Membrane Proteins / genetics
  • Membrane Proteins / physiology*
  • Motor Neurons / drug effects
  • Motor Neurons / metabolism
  • Motor Neurons / physiology
  • Mutation
  • Neuronal Plasticity / genetics
  • Neuronal Plasticity / physiology*
  • Receptor Protein-Tyrosine Kinases / antagonists & inhibitors
  • Receptor Tyrosine Kinase-like Orphan Receptors
  • Receptors, Nicotinic / metabolism
  • Signal Transduction / genetics
  • Signal Transduction / physiology*
  • Synaptic Transmission / physiology*
  • Wnt Proteins / physiology*

Substances

  • Caenorhabditis elegans Proteins
  • Cell Adhesion Molecules
  • Membrane Proteins
  • RIG-3 protein, C elegans
  • Receptors, Nicotinic
  • Wnt Proteins
  • acr-16 protein, C elegans
  • Aldicarb
  • CAM-1 protein, C elegans
  • Receptor Protein-Tyrosine Kinases
  • Receptor Tyrosine Kinase-like Orphan Receptors