Multifunctional potassium channels: electrical switches and redox enzymes, all in one.
Kv1-type K+ channels are protein complexes containing both voltage-sensing, pore-forming alpha subunits and modulatory Kvbeta subunits. Although some Kvbeta subunits include an amino-terminal region that allows them to transform noninactivating Kv1 channels into rapidly inactivating channels, the function of Kvbeta subunits that do not possess these inactivating amino-terminal regions has been less clear. Recent research demonstrates that Kvbeta2 acts as an NADPH (the reduced form of nicotinamide adenine dinucleotide phosphate)-dependent redox enzyme and that its catalytic activity can regulate the speed with which the Kv1.4-Kvbeta2 complex undergoes inactivation, suggesting that Kvbeta2 may link cellular metabolic activity and redox state with electrical signaling.
Heinemann
Stefan H
SH
Center for Molecular Biomedicine, Molecular and Cellular Biophysics, Friedrich Schiller University Jena, D-07747 Jena, Germany. stefan.h.heinemann@uni-jena.de
Hoshi
Toshinori
T
D000429:Alcohol Oxidoreductases / Q000378:metabolism; D000449:Aldehyde Reductase; D000074408:Aldo-Keto Reductases; D000818:Animals; D004553:Electric Conductivity; D008564:Membrane Potentials; D010084:Oxidation-Reduction; D051637:Shaker Superfamily of Potassium Channels / Q000737:chemistry / Q000378:metabolism*
D051637:Shaker Superfamily of Potassium Channels; D000429:Alcohol Oxidoreductases; D000074408:Aldo-Keto Reductases; D000449:Aldehyde Reductase