37
views
0
recommends
+1 Recommend
0 collections
    0
    shares
      • Record: found
      • Abstract: found
      • Article: not found

      Molecular background of leak K+ currents: two-pore domain potassium channels.

      1 ,
      Physiological reviews
      American Physiological Society

      Read this article at

      ScienceOpenPublisherPubMed
      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          Two-pore domain K(+) (K(2P)) channels give rise to leak (also called background) K(+) currents. The well-known role of background K(+) currents is to stabilize the negative resting membrane potential and counterbalance depolarization. However, it has become apparent in the past decade (during the detailed examination of the cloned and corresponding native K(2P) channel types) that this primary hyperpolarizing action is not performed passively. The K(2P) channels are regulated by a wide variety of voltage-independent factors. Basic physicochemical parameters (e.g., pH, temperature, membrane stretch) and also several intracellular signaling pathways substantially and specifically modulate the different members of the six K(2P) channel subfamilies (TWIK, TREK, TASK, TALK, THIK, and TRESK). The deep implication in diverse physiological processes, the circumscribed expression pattern of the different channels, and the interesting pharmacological profile brought the K(2P) channel family into the spotlight. In this review, we focus on the physiological roles of K(2P) channels in the most extensively investigated cell types, with special emphasis on the molecular mechanisms of channel regulation.

          Related collections

          Author and article information

          Journal
          Physiol Rev
          Physiological reviews
          American Physiological Society
          1522-1210
          0031-9333
          Apr 2010
          : 90
          : 2
          Affiliations
          [1 ] Department of Physiology, Semmelweis University, Budapest, Hungary. peter.enyedi@eok.sote.hu
          Article
          90/2/559
          10.1152/physrev.00029.2009
          20393194
          ab44d2f9-89ae-4900-b438-b79493e6efcf
          History

          Comments

          Comment on this article