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Please use this identifier to cite or link to this item: http://dspace.utalca.cl/handle/1950/9487

Title: An Extracellular Ion Pathway Plays a Central Role in the Cooperative Gating of a K-2P K+ Channel by Extracellular pH
Authors: Gonzalez, W.
Zuniga, L.
Cid, L.P.
Arevalo, B.
Niemeyer, M.I.
Sepulveda, F.V.
Issue Date: Feb-2013
Citation: JOURNAL OF BIOLOGICAL CHEMISTRY Volume: 288 Issue: 8 Pages: 5984-5991 DOI: 10.1074/jbc.M112.445528
Abstract: Proton-gated TASK-3K(+) channel belongs to the K-2P family of proteins that underlie the K+ leak setting the membrane potential in all cells. TASK-3 is under cooperative gating control by extracellular [H+]. Use of recently solved K-2P structures allows us to explore the molecular mechanism of TASK-3 cooperative pH gating. Tunnel-like side portals define an extracellular ion pathway to the selectivity filter. We use a combination of molecular modeling and functional assays to show that pH-sensing histidine residues and K+ ions mutually interact electrostatically in the confines of the extracellular ion pathway. K+ ions modulate the pK(a) of sensing histidine side chains whose charge states in turn determine the open/closed transition of the channel pore. Cooperativity, and therefore steep dependence of TASK-3 K+ channel activity on extracellular pH, is dependent on an effect of the permeant ion on the channel pH(o) sensors.
Description: Gonzalez, W (Gonzalez, Wendy). Univ Talca, Ctr Bioinformat & Simulac Mol, Talca 3465548, Chile
URI: http://dspace.utalca.cl/handle/1950/9487
ISSN: 0021-9258
Appears in Collections:Artículos en publicaciones ISI - Universidad de Talca

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