23.09.2020 - A deep-dive into TASK-1
TASK-1: A Two–Pore Domain K+ Channel
Two-pore domain K+ (K2P) channels have been cloned from a variety of species and tissues. They have been characterised biophysically as a ‘background’ K+-selective conductance and are gated by pH, stretch, heat, coupling to G-proteins and anaesthetics. Whilst their precise physiological function is unknown, they are likely to represent an increasingly important family of membrane proteins.
Source: Biochimica et Biophysica Acta (BBA) - Biomembranes Volume 1566, Issues 1–2 (2002). https://doi.org/10.1016/S0005-2736(02)00597-7
Free Application Note: Click here to download the TASK-1 Application Note: Activation and Inhibition of TASK-1
Tandem-Pore Domain Potassium Channels
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 (TRESK)
15 members: K2P1.1 (TWIK-1); K2P2.1 (TREK-1); K2P3.1 (TASK-1); K2P4.1 (TRAAK); K2P5.1 (TASK-2); K2P6.1 (TWIK-2); K2P7.1; K2P9.1 (TASK-3); K2P10.1 (TREK-2); K2P12.1 (THIK-2); K2P13.1 (THIK-1); K2P15.1 (TASK-5); K2P16.1 (TALK-1); K2P17.1 (TASK-2, TASK-4); K2P18.1 (TRIK, TRESK)
The channel protein contains four transmembrane domains, which form two pore loops between domains 1–2 and 3–4. Two subunits associate to form a dimer with bilateral symmetry around the pore. Homodimers and heterodimers are possible.
Several mechanisms including oxygen tension, pH, mechanical stretch, and G-proteins