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.

[3] The two-pore domain potassium channels instead are dimers where each subunit is essentially two α-subunits joined together.

[5] To quote Rang and Dale (2015), "The nomenclature is misleading, especially when they are incorrectly referred to as two-pore channels".

[6] A decrease in these leak channels activity is known as 'channel arrest', which reduces oxygen consumption[7] and allows animals to survive anoxia.

[8] Below is a list of the 15 known two-pore-domain human potassium channels:[1] This protein-related article is a stub.