KCNK dimers transport K+ from cytosol to extracellular region

Stable Identifier
R-HSA-5578910
Type
Reaction [transition]
Species
Homo sapiens
Compartment
ReviewStatus
5/5
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Potassium channels control neuronal excitability through influence over the duration, frequency and amplitude of action potentials. Potassium channels that are active at rest inhibit depolarization toward firing threshold, and thus suppress excitation. Conversely, potassium channels activated at depolarized potentials do not interfere with rise to threshold, but do facilitate recovery and repetitive firing. Tandem pore domain K+ channels (K2p) produce leak K+ current which stabilizes negative membrane potential and counter balances depolarization. These channels are regulated by voltage independent mechanisms such as membrane stretch, pH, temperature (Goldstein et al. 2005, Lotshaw 2007, Enyedi & Czirja 2010). Tandem pore domain K+ channels have been classified into six subfamilies; tandem pore domains in weak rectifying K+ channel (TWIK), TWIK-related K+ channel (TREK), TWIK-related acid-sensitive K+ channel (TASK), TWIK-related alkaline pH-activated K+ channel (TALK), tandem pore domain halothane-inhibted K+ channel (THIK), TWIK-releated spinal cord K+ channel). outwardly rectifying channel that is sensitive to changes in extracellular pH and is inhibited by extracellular acidification. Also referred to as an acid-sensitive potassium channel, it is activated by the anesthetics halothane and isoflurane.
Literature References
PubMed ID Title Journal Year
16382106 International Union of Pharmacology. LV. Nomenclature and molecular relationships of two-P potassium channels

Kim, D, Goldstein, SA, Rajan, S, Plant, LD, Bayliss, DA, Lesage, F

Pharmacol. Rev. 2005
20393194 Molecular background of leak K+ currents: two-pore domain potassium channels

Czirják, G, Enyedi, P

Physiol Rev 2010
17652773 Biophysical, pharmacological, and functional characteristics of cloned and native mammalian two-pore domain K+ channels

Lotshaw, DP

Cell Biochem. Biophys. 2007
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Participates
Catalyst Activity

potassium channel activity of KCNK dimers [plasma membrane]

Orthologous Events
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Rhea
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