Potassium two pore domain channel subfamily K member 15 (KCNK15)

Potassium two pore domain channel subfamily K member 15 (KCNK15, also known as TASK-5) is a member of the two pore domain potassium (K2P) channel family. While isolated KCNK15 (TASK-5) subunits do not form functional homomeric channels, they can form heteromeric channel complexes with TASK-1 and TASK-3, which then display unique electrophysiological and pharmacological properties. These heterodimers are found in various tissues, including the heart, vascular smooth muscle, pancreas, liver, lung, ovary, and testis. TASK-5 modulates the cell surface expression and function of TASK-1 and TASK-3 channels. Its unique association with physiological and disease processes, especially in cardiovascular disease, cancer, and sleep apnea, suggests emerging relevance as a therapeutic target, though there are currently no approved drugs targeting KCNK15 specifically. Key facts: - Not a functional potassium channel as a homodimer; requires co-assembly with TASK-1 or TASK-3 for activity. - Co-expression alters channel surface expression, conductance, and responsiveness to pharmacological modulators. - Genetic polymorphisms in KCNK15 may serve as biomarkers for patient stratification in TASK channel-targeted therapy.

Other names

TASK-5TASK5K2P15.1KT3.3DJ781B1.1Potassium channel, two pore domain subfamily K, member 15Acid-sensitive potassium channel protein TASK-5TWIK-related acid-sensitive K(+) channel 5

Modulation of potassium channel function via heteromeric complex formation (with TASK-1/TASK-3) can affect the pharmacological response and channel conductance properties. Gq-coupled receptor-mediated inhibition of heteromeric channels may be altered.