Parallel Processing of Two Mechanosensory Modalities by a Single Neuron in C. elegans

Dev Cell. 2019 Dec 2;51(5):617-631.e3. doi: 10.1016/j.devcel.2019.10.008. Epub 2019 Nov 14.


Neurons convert synaptic or sensory inputs into cellular outputs. It is not well understood how a single neuron senses, processes multiple stimuli, and generates distinct neuronal outcomes. Here, we describe the mechanism by which the C. elegans PVD neurons sense two mechanical stimuli: external touch and proprioceptive body movement. These two stimuli are detected by distinct mechanosensitive DEG/ENaC/ASIC channels, which trigger distinct cellular outputs linked to mechanonociception and proprioception. Mechanonociception depends on DEGT-1 and activates PVD's downstream command interneurons through its axon, while proprioception depends on DEL-1, UNC-8, and MEC-10 to induce local dendritic Ca2+ increase and dendritic release of a neuropeptide NLP-12. NLP-12 directly modulates neuromuscular junction activity through the cholecystokinin receptor homolog on motor axons, setting muscle tone and movement vigor. Thus, the same neuron simultaneously uses both its axon and dendrites as output apparatus to drive distinct sensorimotor outcomes.

Keywords: C. elegans; ENaC; neuropeptide; polymodal; proprioception.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Axons / metabolism
  • Axons / physiology
  • Caenorhabditis elegans
  • Caenorhabditis elegans Proteins / metabolism
  • Calcium / metabolism
  • Dendrites / metabolism
  • Dendrites / physiology
  • Epithelial Sodium Channels / metabolism
  • Feedback, Physiological
  • Ion Channels / metabolism
  • Mechanotransduction, Cellular*
  • Membrane Proteins / metabolism
  • Neuromuscular Junction / metabolism
  • Neuromuscular Junction / physiology
  • Neuropeptides / metabolism*
  • Proprioception*
  • Sensory Receptor Cells / metabolism*
  • Sensory Receptor Cells / physiology


  • Caenorhabditis elegans Proteins
  • Epithelial Sodium Channels
  • Ion Channels
  • Membrane Proteins
  • Neuropeptides
  • unc-8 protein, C elegans
  • MEC-10 protein, C elegans
  • Calcium