Identification of a novel tetramerization domain in large conductance K(ca) channels

Neuron. 2001 Oct 11;32(1):13-23. doi: 10.1016/s0896-6273(01)00444-5.


More than 50 genes are known to encode K(+) channel monomers and can coassemble to form hetero-tetrameric K(+) channels. However, only a subset of possible monomer combinations come together to form functional ion channels. The assembly and tetramerization of appropriate channel monomers is mediated by association domains (ADs). To identify such domains in human large-conductance Ca(2+)-activated K(+) channels (hSlo1), we screened hSlo1 domains for self-association using yeast two-hybrid assays. Putative ADs were subjected to functional assays in Xenopus oocytes and further characterized by coprecipitation, native gel electrophoresis, and sucrose density gradient centrifugation assays. This led to the identification of a single intracellular association domain localized near the channel pore and required for channel function. We conclude that this novel tetramerization domain, referred to as BK-T1, promotes the assembly of hSlo1 monomers into functional K(Ca) channels.

Publication types

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

MeSH terms

  • Animals
  • Conserved Sequence
  • Humans
  • Ion Channel Gating / physiology*
  • Large-Conductance Calcium-Activated Potassium Channels
  • Molecular Sequence Data
  • Mutagenesis / physiology
  • Oocytes / physiology
  • Potassium Channels / chemistry*
  • Potassium Channels / genetics*
  • Potassium Channels / metabolism
  • Potassium Channels, Calcium-Activated*
  • Protein Structure, Tertiary
  • Sequence Homology, Amino Acid
  • Two-Hybrid System Techniques
  • Xenopus laevis
  • Yeasts


  • Large-Conductance Calcium-Activated Potassium Channels
  • Potassium Channels
  • Potassium Channels, Calcium-Activated