Potassium leak channels and the KCNK family of two-P-domain subunits.
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.
Department of Pediatrics and Cellular and Molecular Physiology, Boyer Center for Molecular Medicine, Yale University School of Medicine, New Haven, Connecticut 06536, USA. steve.goldstein@yale.edu
S A
SA
Goldstein
D
D
Bockenhauer
I
I
O'Kelly
N
N
Zilberberg
D000818:Animals; D004594:Electrophysiology; D006801:Humans; D008958:Models, Molecular; D009206:Myocardium / Q000378:metabolism; D009419:Nerve Tissue Proteins; D009474:Neurons / Q000378:metabolism; D009865:Oocytes / Q000502:physiology; D018408:Patch-Clamp Techniques; D011188:Potassium / Q000378:metabolism*; D015221:Potassium Channels / Q000737:chemistry / Q000235:genetics / Q000502:physiology*; D024683:Potassium Channels, Tandem Pore Domain; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D021122:Protein Subunits
D009419:Nerve Tissue Proteins; D015221:Potassium Channels; D024683:Potassium Channels, Tandem Pore Domain; D021122:Protein Subunits; C420132:potassium channel subfamily K member 3; D011188:Potassium