The DRASIC cation channel contributes to the detection of cutaneous touch and acid stimuli in mice

Neuron. 2001 Dec 20;32(6):1071-83. doi: 10.1016/s0896-6273(01)00547-5.


Cation channels in the DEG/ENaC family are proposed to detect cutaneous stimuli in mammals. We localized one such channel, DRASIC, in several different specialized sensory nerve endings of skin, suggesting it might participate in mechanosensation and/or acid-evoked nociception. Disrupting the mouse DRASIC gene altered sensory transduction in specific and distinct ways. Loss of DRASIC increased the sensitivity of mechanoreceptors detecting light touch, but it reduced the sensitivity of a mechanoreceptor responding to noxious pinch and decreased the response of acid- and noxious heat-sensitive nociceptors. The data suggest that DRASIC subunits participate in heteromultimeric channel complexes in sensory neurons. Moreover, in different cellular contexts, DRASIC may respond to mechanical stimuli or to low pH to mediate normal touch and pain sensation.

Publication types

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

MeSH terms

  • Acid Sensing Ion Channels
  • Acids
  • Animals
  • Behavior, Animal / physiology
  • Hot Temperature
  • Mechanoreceptors / physiology
  • Membrane Potentials / physiology
  • Membrane Proteins*
  • Mice
  • Mice, Inbred C57BL
  • Mice, Knockout
  • Nerve Endings / physiology
  • Nerve Tissue Proteins / genetics
  • Nerve Tissue Proteins / metabolism
  • Neurons, Afferent / physiology
  • Nociceptors / physiology
  • Pain / chemically induced
  • Pain / physiopathology
  • Patch-Clamp Techniques
  • Physical Stimulation
  • Recombination, Genetic
  • Sodium Channels / genetics*
  • Sodium Channels / metabolism*
  • Stimulation, Chemical
  • Touch / physiology*


  • ASIC3 protein, human
  • Acid Sensing Ion Channels
  • Acids
  • Membrane Proteins
  • Nerve Tissue Proteins
  • Sodium Channels