KCNE1 binds to the KCNQ1 pore to regulate potassium channel activity

Neuron. 2004 Jun 24;42(6):927-37. doi: 10.1016/j.neuron.2004.06.001.


Potassium channels control the resting membrane potential and excitability of biological tissues. Many voltage-gated potassium channels are controlled through interactions with accessory subunits of the KCNE family through mechanisms still not known. Gating of mammalian channel KCNQ1 is dramatically regulated by KCNE subunits. We have found that multiple segments of the channel pore structure bind to the accessory protein KCNE1. The sites that confer KCNE1 binding are necessary for the functional interaction, and all sites must be present in the channel together for proper regulation by the accessory subunit. Specific gating control is localized to a single site of interaction between the ion channel and accessory subunit. Thus, direct physical interaction with the ion channel pore is the basis of KCNE1 regulation of K+ channels.

Publication types

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

MeSH terms

  • Animals
  • Blotting, Western / methods
  • Cell Line
  • Cricetinae
  • Cricetulus
  • Electric Conductivity
  • Embryo, Mammalian
  • Fluorescent Antibody Technique / methods
  • Humans
  • Ion Channel Gating
  • KCNQ Potassium Channels
  • KCNQ1 Potassium Channel
  • Kidney
  • Membrane Potentials / physiology
  • Models, Molecular
  • Mutagenesis, Site-Directed
  • Patch-Clamp Techniques / methods
  • Potassium Channels / chemistry*
  • Potassium Channels / metabolism*
  • Potassium Channels, Voltage-Gated*
  • Precipitin Tests / methods
  • Protein Binding
  • Recombinant Fusion Proteins / metabolism
  • Structure-Activity Relationship
  • Transfection / methods


  • KCNQ Potassium Channels
  • KCNQ1 Potassium Channel
  • KCNQ1 protein, human
  • Potassium Channels
  • Potassium Channels, Voltage-Gated
  • Recombinant Fusion Proteins
  • potassium channel protein I(sk)