A family of K+ channel ancillary subunits regulate taste sensitivity in Caenorhabditis elegans

J Biol Chem. 2005 Jun 10;280(23):21893-9. doi: 10.1074/jbc.M502732200. Epub 2005 Mar 30.

Abstract

We have identified a family of ancillary subunits of K(+) channels in Caenorhabditis elegans. MPS-1 and its related members MPS-2, MPS-3, and MPS-4 are detected in the nervous system of the nematode. Electrophysiological analysis in ASE neurons and mammalian cells and epigenetic inactivation by double-stranded RNA interference (RNAi) in vivo show that each MPS can associate with and functionally endow the voltage-gated K(+) channel KVS-1. In the chemosensory neuron ADF, three different MPS subunits combine with KVS-1 to form both binary (MPS-1.KVS-1) and ternary (MPS-2.MPS-3.KVS-1) complexes. RNAi of mps-2, mps-3, or both, enhance the taste of the animal for sodium without altering the susceptibility to other attractants. When sodium is introduced in the test plate as background or as antagonist attractant, the nematode loses the ability to recognize a second attractant. Thus, it appears that the chemosensory apparatus of C. elegans uses sensory thresholds and that a voltage-gated K(+) channel is specifically required for this mechanism.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Animals, Genetically Modified
  • CHO Cells
  • Caenorhabditis elegans / metabolism*
  • Caenorhabditis elegans Proteins / physiology
  • Cloning, Molecular
  • Coloring Agents / pharmacology
  • Cricetinae
  • Cyclic AMP / metabolism
  • DNA, Complementary / metabolism
  • Electrophysiology
  • Green Fluorescent Proteins / chemistry
  • Membrane Proteins / physiology
  • Molecular Sequence Data
  • Neurons / metabolism
  • Nuclear Proteins / physiology
  • Phenotype
  • Potassium / chemistry
  • Potassium Channels / chemistry*
  • Potassium Channels / physiology
  • Protein Binding
  • RNA Interference
  • RNA, Double-Stranded / chemistry
  • Saccharomyces cerevisiae Proteins / physiology
  • Sodium / pharmacology
  • Time Factors

Substances

  • Caenorhabditis elegans Proteins
  • Coloring Agents
  • DNA, Complementary
  • MPS-1 protein, C elegans
  • MPS2 protein, S cerevisiae
  • Membrane Proteins
  • Mps3 protein, S cerevisiae
  • Nuclear Proteins
  • Potassium Channels
  • RNA, Double-Stranded
  • Saccharomyces cerevisiae Proteins
  • Green Fluorescent Proteins
  • Sodium
  • Cyclic AMP
  • Potassium