The two-pore-domain or tandem pore domain potassium channels are a family of 15 members that form what is known as leak channels which possess Goldman-Hodgkin-Katz (open) rectification. These channels are regulated by several mechanisms including signaling lipids, oxygen tension, pH, mechanical stretch, and G-proteins. Two-pore-domain potassium channels correspond structurally to a inward-rectifier potassium channel α-subunits. Each inward-rectifier potassium channel α-subunit is composed of two transmembrane α-helices, a pore helix and a potassium ion selectivity filter sequence and assembles into a tetramer forming the complete channel. The two-pore domain potassium channels instead are dimers where each subunit is essentially two α-subunits joined together.
Each single channel does not have two pores; the name of the channel comes from the fact that each subunit has two P (pore) domains in its primary sequence. To quote Rang and Dale (2015), "The nomenclature is misleading, especially when they are incorrectly referred to as two-pore channels".
A decrease in these leak channels activity is known as 'channel arrest', which reduces oxygen consumption and allows animals to survive anoxia.
Below is a list of the 15 known two-pore-domain human potassium channels:
| Gene | Channel | Family | Aliases |
| KCNK1 | K2p1.1 | TWIK | TWIK-1 |
| KCNK2 | K2p2.1 | TREK | TREK-1 |
| KCNK3 | K2p3.1 | TASK | TASK-1 |
| KCNK4 | K2p4.1 | TREK | TRAAK |
| KCNK5 | K2p5.1 | TASK | TASK-2 |
| KCNK6 | K2p6.1 | TWIK | TWIK-2 |
| KCNK7 | K2p7.1 | TWIK | |
| KCNK9 | K2p9.1 | TASK | TASK-3 |
| KCNK10 | K2p10.1 | TREK | TREK-2 |
| KCNK12 | K2p12.1 | THIK | THIK-2 |
| KCNK13 | K2p13.1 | THIK | THIK-1 |
| KCNK15 | K2p15.1 | TASK | TASK-5 |
| KCNK16 | K2p16.1 | TALK | TALK-1 |
| KCNK17 | K2p17.1 | TALK | TALK-2, TASK-4 |
| KCNK18 | K2p18.1 | TRIK, TRESK |
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See also
- Ion channel
- Potassium channel
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