Tandem pore domain potassium channel

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 . Their name is derived from the fact that the α subunits consist of four transmembrane segments, each containing two pore loops. As such, they structurally correspond to two inward-rectifier α subunits and thus form dimers in the membrane. 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 . Their name is derived from the fact that the α subunits consist of four transmembrane segments, each containing two pore loops. As such, they structurally correspond to two inward-rectifier α subunits and thus form dimers in the membrane. 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 ismisleading, especially when they are incorrectly referred to as two-pore channels'. Below is a list of the 15 known two-pore-domain human potassium channels:

[ "Voltage-gated ion channel", "KcsA potassium channel", "Voltage-gated potassium channel" ]
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