Voltage-dependent potassium channel subfamily KQT member 2 (Kv7.2)

The voltage-dependent potassium channel subfamily KQT member 2 (Kv7.2, encoded by the KCNQ2 gene) is a tetrameric membrane protein that forms a voltage-gated potassium ion (K⁺) channel, crucial for the regulation of neuronal excitability. Kv7.2, often coassembled with Kv7.3, creates the molecular basis of the neuronal M-current that acts as a ‘brake’ on excessive neuronal firing. Each α subunit contains six transmembrane segments with distinct voltage-sensing and pore-forming domains, and a large cytosolic C-terminus involved in protein-protein interactions, including binding to calmodulin and other regulators. Mutations in KCNQ2 are a major cause of benign familial neonatal seizures as well as severe early-onset epileptic encephalopathies. Kv7.2 channels are targets for anti-epileptic drugs such as retigabine, which act by stabilizing the open conformation of the channel, thereby enhancing the M-current and reducing neuronal hyperexcitability[1][3][4].

Other names

KCNQ2Kv7.2M-channel subunit Kv7.2Potassium channel subfamily KQT member 2

Positive allosteric modulation of the potassium current (channel opening stabilization); Inhibition/antagonism of the channel (blockers reduce the M-current and increase excitability)