title: KCNK2: reversible conversion of a hippocampal potassium leak into a voltage-dependent channel.
abstract: Potassium leak channels are essential to neurophysiological function. Leaks suppress excitability through maintenance of resting membrane potential below the threshold for action potential firing. Conversely, voltage-dependent potassium channels permit excitation because they do not interfere with rise to threshold, and they actively promote recovery and rapid re-firing. Previously attributed to distinct transport pathways, we demonstrate here that phosphorylation of single, native hippocampal and cloned KCNK2 potassium channels produces reversible interconversion between leak and voltage-dependent phenotypes. The findings reveal a pathway for dynamic regulation of excitability.
authors.affiliation: Departments of Pediatrics and Cellular and Molecular Physiology, Boyer Center for Molecular Medicine, Yale University School of Medicine, New Haven, Connecticut 06536, USA.
authors.forename: D
authors.initials: D
authors.lastname: Bockenhauer
authors.forename: N
authors.initials: N
authors.lastname: Zilberberg
authors.forename: S A
authors.initials: SA
authors.lastname: Goldstein
mesh_terms: D000818:Animals; D003001:Cloning, Molecular; D017868:Cyclic AMP-Dependent Protein Kinases / Q000378:metabolism; D004594:Electrophysiology; D006624:Hippocampus / Q000378:metabolism*; D006801:Humans; D009865:Oocytes / Q000378:metabolism; D018408:Patch-Clamp Techniques; D010641:Phenotype; D010766:Phosphorylation; D011188:Potassium / Q000378:metabolism*; D015221:Potassium Channels / Q000235:genetics / Q000378:metabolism*; D024683:Potassium Channels, Tandem Pore Domain; D051381:Rats; D014982:Xenopus laevis
chemical_list: D015221:Potassium Channels; D024683:Potassium Channels, Tandem Pore Domain; C103742:potassium channel protein TREK-1; D017868:Cyclic AMP-Dependent Protein Kinases; D011188:Potassium