Potassium channel, subfamily K, member 13 (KCNK13), also known as K2P13.1 or THIK-1, is a protein that in humans is encoded by the KCNK13gene. It is a potassium channel containing two pore-forming P domains.[5][6]
Ribbon structure of homodimeric two-pore potassium channel K2P13 (THIK-1).
K2P13.1 was first discovered in 2000 from a rat cDNA library, along with the closely related protein K2P12.1[5] The two channels were named tandem pore domain halothane-inhibited K+ channel 1 and 2 (THIK-1 and THIK-2) because the anesthetichalothane inhibited the potassium current. THIK-1 was also shown to be activated by arachidonic acid and displayed mild voltage dependence, with moderate outward rectification at low external K+ and weak inward rectification with nearly symmetrical K+ concentrations.[5][8] Later research showed that THIK-1 can be activated by G-protein-coupled receptor pathways[9] and by polyanionic lipids such as PIP2 and oleoyl-CoA.[10]
In humans, THIK-1 expression is almost exclusively restricted to microglia, where it functions as the main potassium channel and is responsible for maintaining their resting membrane potential through tonic background potassium conductance.[11] THIK-1 activity can regulate microglial ramification, surveillance, NLRP3inflammasome activation, and subsequent release of pro-inflammatory cytokine interleukin-1β (IL-1β).[12][13][14] It also plays a role in cell shrinkage during apoptosis via caspase-8 cleavage.[15]
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