The MEC-4 DEG/ENaC channel of Caenorhabditis elegans touch receptor neurons transduces mechanical signals

Nat Neurosci. 2005 Jan;8(1):43-50. doi: 10.1038/nn1362. Epub 2004 Dec 5.


Transformation of mechanical energy into ionic currents is essential for touch, hearing and nociception. Although DEG/ENaC proteins are believed to form sensory mechanotransduction channels, the evidence for this role remains indirect. By recording from C. elegans touch receptor neurons in vivo, we found that external force evokes rapidly activating mechanoreceptor currents (MRCs) carried mostly by Na(+) and blocked by amiloride-characteristics consistent with direct mechanical gating of a DEG/ENaC channel. Like mammalian Pacinian corpuscles, these neurons depolarized with both positive and negative changes in external force but not with sustained force. Null mutations in the DEG/ENaC gene mec-4 and in the accessory ion channel subunit genes mec-2 and mec-6 eliminated MRCs. In contrast, the genetic elimination of touch neuron-specific microtubules reduced, but did not abolish, MRCs. Our findings link the application of external force to the activation of a molecularly defined metazoan sensory transduction channel.

Publication types

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

MeSH terms

  • Amiloride / pharmacology
  • Animals
  • Caenorhabditis elegans Proteins / genetics
  • Caenorhabditis elegans Proteins / metabolism*
  • Caenorhabditis elegans*
  • Electric Conductivity
  • Mechanoreceptors / drug effects
  • Mechanoreceptors / physiology*
  • Mechanotransduction, Cellular / physiology*
  • Membrane Proteins / genetics
  • Membrane Proteins / metabolism*
  • Mutation / physiology
  • Physical Stimulation
  • Sodium / pharmacology
  • Sodium Channels / metabolism*
  • Touch / physiology*


  • Caenorhabditis elegans Proteins
  • Deg-1 protein, C elegans
  • Mec-4 protein, C elegans
  • Membrane Proteins
  • Sodium Channels
  • Amiloride
  • Sodium