Potassium two pore domain channel subfamily K member 10 (KCNK10)

Potassium two pore domain channel subfamily K member 10 (KCNK10), also known as TREK-2, is a protein that forms potassium-selective leak channels containing two pore-forming P domains per subunit, distinguishing it as a member of the K2P channel family[1][3]. It mainly passes outward potassium currents under physiological conditions and is strongly stimulated by arachidonic acid, general anesthetics, heat, mechanical stretch, and intracellular acidification[1]. Functionally, KCNK10 stabilizes the resting membrane potential of neurons and is involved in the regulation of cellular excitability, pain sensation, and neurogenic inflammation by forming homo- or heterodimers with other K2P family members including TRESK[1][2]. It is associated with neurological development and functions, and mutations or dysregulation have been linked to diseases such as Birk-Barel syndrome and some cancers[1][4]. Known to be modulated indirectly by drugs like general anesthetics and certain antidepressants, KCNK10 is considered a therapeutic target due to its critical role in regulating neuronal activity and potential involvement in pain modulation[1][2].

Other names

KCNK10TREK-2TREK2K2p10.1PPP1R97Outward rectifying potassium channel protein TREK-2TWIK-related K+ channel 2potassium channel subfamily K member 102P domain potassium channel TREK2TREK2 K(+) channel subunitpotassium channel TREK-2protein phosphatase 1 regulatory subunit 97

Channel agonists/activators stabilize open/leak conductance state, hyperpolarizing neurons and reducing excitability. Channel inhibitors/antagonists reduce conductance, increasing neuronal activity. Anesthetics enhance potassium flux to decrease neuronal firing.