Article
Determinants of pH sensing in the two-pore domain K(+) channels TASK-1 and -2.
Pflugers Archiv : European journal of physiology - 1 Feb 2003
Morton Michael J, O'Connell Anthony D, Sivaprasadarao Asipu, Hunter Malcolm
Abstract excerpt
TASK-1 and -2 are members of the two-pore domain potassium (K(+)) channel family and are sensitive to changes in extracellular pH. The effects of mutating charged, extracellular-facing residues in TASK-1 and -2 were studied in Xenopusoocytes by two-electrode voltage clamp. Hydrogen ion block was independent of voltage with K(d) values of 149+/-17.9 nM [H(+)] ( n=6) and 5.76+/-1.23 nM [H(+)] ( n=7) for TASK-1 and...
Topics
- Amino Acid Sequence
- Animals
- Biosensing Techniques
- Electric Conductivity
- Electrophysiology
- Extracellular Space
- Female
- Humans
- Hydrogen-Ion Concentration
- Mice
- Molecular Sequence Data
- Mutation
- Nerve Tissue Proteins
- Oocytes
- Patch-Clamp Techniques
- Potassium Channels
- Potassium Channels, Tandem Pore Domain
- Protein Structure, Tertiary