K+ transport characteristics of the plasma membrane tandem-pore channel TPK4 and pore chimeras with its vacuolar homologs

FEBS Lett. 2010 Jun 3;584(11):2433-9. doi: 10.1016/j.febslet.2010.04.038. Epub 2010 Apr 20.


Vacuolar tandem-pore channels could not be analysed in Xenopus oocytes so far, due to misguided translocation. Owing to the conservation of their pore regions, we were able to prepare functional pore-chimeras between the plasma membrane localised TPK4 and vacuolar TPKs. Thereby, we found evidence that TPK2, TPK3 and TPK5, just like TPK4, form potassium-selective channels with instantaneous current kinetics. Homology modelling and mutational analyses identified a pore-located aspartate residue (Asp110), which is involved in potassium permeation as well as in inward rectification of TPK4. Furthermore, dominant-negative mutations in the selectivity filter of either pore one or two (Asp86,Asp200) rendered TPK4 non-functional. This observation supports the notion that the functional TPK4 channel complex is formed by two subunits.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Biological Transport
  • Cell Membrane / metabolism*
  • Cellular Structures / metabolism
  • Chimera / metabolism*
  • Ion Channels / metabolism*
  • Kinetics
  • Potassium / metabolism*
  • Potassium Channels / chemistry
  • Potassium Channels / genetics
  • Potassium Channels / metabolism*
  • Vacuoles / metabolism


  • Ion Channels
  • Potassium Channels
  • Potassium