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Design
Editorial
This editorial highlights the growing recognition of Kv7 channels' physiological roles and pharmacological potential beyond their traditional classification as purely cardiac or neuronal channels.
The Kv7 family of voltage-gated potassium (K + ) channels consists of five members (Kv7.1-7.5) encoded for by the KCNQ1-5 genes, respectively. Kv7 channels assemble as tetramers of identical or compatible subunits, with each subunit consisting of six transmembrane segments (S1-S6) and cytoplasmic N-and C-termini. The transmembrane segments between S1 and S4 form the voltage-sensing domain (VSD), where the S4 segment is crucial for channel gating as it contains positively charged arginines (Rs), each separated by non-polar residues. The S5 and S6 segments and the interconnecting loop participate to the formation of the pore domain (PD). Kv7 channels are characterized by a long intracellular C-terminus, containing domains necessary for tetramerization and involved in binding and transductional activity by critical regulators, such as phosphatidylinositol 4,5-bisphosphate (PIP2), calmodulin (CaM), syntaxin, A-kinase-anchoring proteins and proteinkinase C, and ankyrin-G (
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Jepps et al. (2021) studied this question.
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