The pore structure and gating mechanism of K2P channels

• Paula L Piechotta ^[2] ; Markus Rapedius ^[3] ; Phillip J Stansfeld ^[1] ; Murali K Bollepalli ^[3] ; Gunter Erhlich ^[2] ; Isabelle Andres-Enguix ^[1] ; Hariolf Fritzenschaft ^[3] ; Niels Decher ^[4] ; Mark S P Sansom ^[1] ; Stephen J Tucker ^[1] ; Thomas Baukrowitz ^[3]
  1. [1] University of Oxford

     University of Oxford

     Oxford District, Reino Unido

     
  2. [2] Universitätsklinikum Jena, Institute of Physiology II, Jena, Germany
  3. [3] Institute of Physiology, Christian-Albrechts University, Kiel, Germany
  4. [4] Institute of Physiology and Pathophysiology, University of Marburg, Marburg, Germany

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• Localización: EMBO journal: European Molecular Biology Organization, ISSN 0261-4189, Vol. 30, Nº. 17, 2011, págs. 3607-3619
• Idioma: inglés
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• Resumen

  • K2P potassium channels are important regulators of cellular excitability. This study reveals that in contrast to most other K+ channels the primary gating mechanism in the K2P channel TREK-1 does not involve opening and closure of the cytoplasmic bundle crossing, but takes place close to or within the selectivity filter.