title: External K+ modulates the activity of the Arabidopsis potassium channel SKOR via an unusual mechanism.
abstract: Plant outward-rectifying K+ channels mediate K+ efflux from guard cells during stomatal closure and from root cells into the xylem for root-shoot allocation of potassium (K). Intriguingly, the gating of these channels depends on the extracellular K+ concentration, although the ions carrying the current are derived from inside the cell. This K+ dependence confers a sensitivity to the extracellular K+ concentration ([K+]) that ensures that the channels mediate K+ efflux only, regardless of the [K+] prevailing outside. We investigated the mechanism of K+-dependent gating of the K+ channel SKOR of Arabidopsis by site-directed mutagenesis. Mutations affecting the intrinsic K+ dependence of gating were found to cluster in the pore and within the sixth transmembrane helix (S6), identifying an 'S6 gating domain' deep within the membrane. Mapping the SKOR sequence to the crystal structure of the voltage-dependent K+ channel KvAP from Aeropyrum pernix suggested interaction between the S6 gating domain and the base of the pore helix, a prediction supported by mutations at this site. These results offer a unique insight into the molecular basis for a physiologically important K+-sensory process in plants.
authors.affiliation: Laboratory of Plant Physiology and Biophysics, IBLS Plant Sciences, Bower Building, University of Glasgow, Glasgow G12 8QQ, UK.
authors.forename: Ingela
authors.initials: I
authors.lastname: Johansson
authors.forename: Klaas
authors.initials: K
authors.lastname: Wulfetange
authors.forename: Fabien
authors.initials: F
authors.lastname: Porée
authors.forename: Erwan
authors.initials: E
authors.lastname: Michard
authors.forename: Pawel
authors.initials: P
authors.lastname: Gajdanowicz
authors.forename: Benoît
authors.initials: B
authors.lastname: Lacombe
authors.forename: Hervé
authors.initials: H
authors.lastname: Sentenac
authors.forename: Jean-Baptiste
authors.initials: JB
authors.lastname: Thibaud
authors.forename: Bernd
authors.initials: B
authors.lastname: Mueller-Roeber
authors.forename: Michael R
authors.initials: MR
authors.lastname: Blatt
authors.forename: Ingo
authors.initials: I
authors.lastname: Dreyer
mesh_terms: D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D017360:Arabidopsis / Q000235:genetics / Q000502:physiology*; D029681:Arabidopsis Proteins / Q000737:chemistry / Q000187:drug effects / Q000235:genetics / Q000502:physiology*; D015640:Ion Channel Gating / Q000502:physiology; D008564:Membrane Potentials / Q000502:physiology; D008958:Models, Molecular; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D011188:Potassium / Q000494:pharmacology*; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000378:metabolism; D051637:Shaker Superfamily of Potassium Channels / Q000737:chemistry / Q000187:drug effects / Q000235:genetics / Q000502:physiology*
chemical_list: D029681:Arabidopsis Proteins; D011994:Recombinant Proteins; C114544:SKOR protein, Arabidopsis; D051637:Shaker Superfamily of Potassium Channels; D011188:Potassium