Decoding of polymodal sensory stimuli by postsynaptic glutamate receptors in C. elegans

Neuron. 2002 Dec 5;36(5):933-44. doi: 10.1016/s0896-6273(02)01088-7.

Abstract

The C. elegans polymodal ASH sensory neurons detect mechanical, osmotic, and chemical stimuli and release glutamate to signal avoidance responses. To investigate the mechanisms of this polymodal signaling, we have characterized the role of postsynaptic glutamate receptors in mediating the response to these distinct stimuli. By studying the behavioral and electrophysiological properties of worms defective for non-NMDA (GLR-1 and GLR-2) and NMDA (NMR-1) receptor subunits, we show that while the osmotic avoidance response requires both NMDA and non-NMDA receptors, the response to mechanical stimuli only requires non-NMDA receptors. Furthermore, analysis of the EGL-3 proprotein convertase provides additional evidence that polymodal signaling in C. elegans occurs via the differential activation of postsynaptic glutamate receptor subtypes.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Behavior, Animal / physiology
  • Caenorhabditis elegans / physiology*
  • Caenorhabditis elegans Proteins / genetics
  • Caenorhabditis elegans Proteins / metabolism
  • Cations / metabolism
  • Electrophysiology
  • Excitatory Amino Acid Agonists / pharmacology
  • Ion Channel Gating / physiology
  • Luminescent Proteins / genetics
  • Luminescent Proteins / metabolism
  • Models, Biological
  • Molecular Sequence Data
  • Mutation
  • N-Methylaspartate / pharmacology
  • Neurons, Afferent / cytology
  • Neurons, Afferent / drug effects
  • Neurons, Afferent / metabolism*
  • Physical Stimulation*
  • Protein Subunits / genetics
  • Protein Subunits / metabolism
  • Receptors, AMPA / genetics
  • Receptors, AMPA / metabolism*
  • Receptors, N-Methyl-D-Aspartate / genetics
  • Receptors, N-Methyl-D-Aspartate / metabolism*
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / metabolism
  • Signal Transduction / physiology
  • Stimulation, Chemical*
  • alpha-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid / pharmacology

Substances

  • Caenorhabditis elegans Proteins
  • Cations
  • Excitatory Amino Acid Agonists
  • Luminescent Proteins
  • Protein Subunits
  • Receptors, AMPA
  • Receptors, N-Methyl-D-Aspartate
  • Recombinant Fusion Proteins
  • N-Methylaspartate
  • alpha-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid