Potassium leak channels and the KCNK family of two-P-domain subunits

Nat Rev Neurosci. 2001 Mar;2(3):175-84. doi: 10.1038/35058574.

Abstract

With a bang, a new family of potassium channels has exploded into view. Although KCNK channels were discovered only five years ago, they already outnumber other channel types. KCNK channels are easy to identify because of their unique structure--they possess two preforming domains in each subunit. The new channels function in a most remarkable fashion: they are highly regulated, potassium-selective leak channels. Although leak currents are fundamental to the function of nerves and muscles, the molecular basis for this type of conductance had been a mystery. Here we review the discovery of KCNK channels, what has been learned about them and what lies ahead. Even though two-P-domain channels are widespread and essential, they were hidden from sight in plain view--our most basic questions remain to be answered.

Publication types

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

MeSH terms

  • Animals
  • Electrophysiology
  • Humans
  • Models, Molecular
  • Myocardium / metabolism
  • Nerve Tissue Proteins
  • Neurons / metabolism
  • Oocytes / physiology
  • Patch-Clamp Techniques
  • Potassium / metabolism*
  • Potassium Channels / chemistry
  • Potassium Channels / genetics
  • Potassium Channels / physiology*
  • Potassium Channels, Tandem Pore Domain
  • Protein Conformation
  • Protein Structure, Tertiary
  • Protein Subunits

Substances

  • Nerve Tissue Proteins
  • Potassium Channels
  • Potassium Channels, Tandem Pore Domain
  • Protein Subunits
  • potassium channel subfamily K member 3
  • Potassium