Molecular basis of functional diversity of voltage-gated potassium channels in mammalian brain

EMBO J. 1989 Nov;8(11):3235-44. doi: 10.1002/j.1460-2075.1989.tb08483.x.


Cloning and sequencing of cDNAs isolated from a rat cortex cDNA library reveals that a gene family encodes several highly homologous K+ channel forming (RCK) proteins. Functional characterization of the channels expressed in Xenopus laevis oocytes following microinjection of in vitro transcribed RCK-specific RNAs shows that each of the RCK proteins forms K+ channels that differ greatly in both their functional and pharmacological properties. This suggests that the molecular basis for the diversity of voltage-gated K+ channels in mammalian brain is based, at least partly, on the expression of several RCK proteins by a family of genes and their assembly to homooligomeric K+ channels with different functional properties.

MeSH terms

  • 4-Aminopyridine / pharmacology
  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Blotting, Southern
  • Brain / metabolism*
  • Cloning, Molecular
  • DNA / genetics
  • Electric Conductivity
  • Electrophysiology
  • Gene Expression Regulation
  • Ion Channel Gating*
  • Molecular Sequence Data
  • Multigene Family
  • Nerve Tissue Proteins / genetics
  • Nerve Tissue Proteins / metabolism*
  • Potassium Channels / metabolism*
  • Rats
  • Sequence Homology, Nucleic Acid
  • Tetraethylammonium Compounds / pharmacology
  • Xenopus laevis


  • Nerve Tissue Proteins
  • Potassium Channels
  • Tetraethylammonium Compounds
  • DNA
  • 4-Aminopyridine

Associated data

  • GENBANK/X16001
  • GENBANK/X16002
  • GENBANK/X16003