Regulation of voltage dependence of the KAT1 channel by intracellular factors.
The KAT1 channel is a hyperpolarization-activated K+ channel cloned from the higher plant Arabidopsis. The deduced amino acid sequence suggests that its structural organization is similar to that of the Shaker-like K+ channel activated by depolarization. Electrophysiological properties of the KAT1 channel expressed in Xenopus oocytes indicate that voltage-dependent activation of the KAT1 channel is not caused by the divalent ion block and that it is intrinsic to the channel. Activity of the KAT1 channel progressively decreases upon patch excision. This rundown of the channel is accompanied by a large shift in the voltage dependence of the channel to a more negative direction. The voltage dependence is also regulated by pH, ATP, and cGMP.
Hoshi
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Department of Physiology and Biophysics, University of Iowa College of Medicine, Iowa City 52242, USA.
D000255:Adenosine Triphosphate / Q000494:pharmacology; D000818:Animals; D017360:Arabidopsis / Q000235:genetics / Q000378:metabolism; D003001:Cloning, Molecular; D006152:Cyclic GMP / Q000494:pharmacology; D004594:Electrophysiology; D006863:Hydrogen-Ion Concentration; D007425:Intracellular Membranes / Q000502:physiology*; D007700:Kinetics; D009865:Oocytes / Q000378:metabolism; D015221:Potassium Channels / Q000187:drug effects / Q000235:genetics / Q000502:physiology*; D014981:Xenopus
D015221:Potassium Channels; D000255:Adenosine Triphosphate; D006152:Cyclic GMP