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Please use this identifier to cite or link to this item: http://dspace.utalca.cl/handle/1950/4505

Title: Gating of two-pore domain K+ channels by extracellular pH
Authors: Niemeyer, M.I.
González-Nilo, F.
Zúniga, L.
González, W.
Cid, L.P.
Sepúlveda, F.V.
Keywords: extracellular pH; gating; KCNK channel; K+ channel; TALK channel; TASK-2 channel
Issue Date: 2006
Publisher: Portland Press on behalf of The Biochemical Society
Citation: Biochemical Society Transactions 34: 899-902
Abstract: Potassium channels have a conserved selectivity filter that is important in determining which ions are conducted and at what rate. Although K+ channels of different conductance characteristics are known, they differ more widely in the way their opening and closing, the gating, is governed. TASK and TALK subfamily proteins are two-pore region KCNK K+ channels gated open by extracellular pH. We discuss the mechanism for this gating in terms of electrostatic effects on the pore changing the occupancy and open probability of the channels in a way reminiscent of C-type inactivation gating at the selectivity filter. Essential to this proposed mechanism is the replacement of two highly conserved aspartate residues at the pore mouth by asparagine or histidine residues in the TALK and TASK channels.
Description: M.I. Niemeyer*, F.D. González-Nilo†, L. Zúñiga*, W. González†, L.P. Cid* and F.V. Sepúlveda* *CECS (Centro de Estudios Científicos), Av. Arturo Prat 514, Valdivia, Chile, †Centro de Bioinformática y Simulación Molecular, Universidad de Talca, 2 Norte 685, Talca, Chile, and ‡Universidad Austral de Chile, Valdivia, Chile
URI: http://dspace.utalca.cl/handle/1950/4505
ISSN: 0300-5127
Appears in Collections:Artículos en publicaciones ISI - Universidad de Talca

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