Phosphorylation of the Kv7.4 B helix reorganizes calmodulin interactions and reduces PIP2 binding
Voltage-gated Kv7 (KCNQ, M-type) potassium channels regulate cellular excitability through interactions with phosphatidylinositol 4,5-bisphosphate (PIP2) and calmodulin (CaM). The distal B helix of Kv7.2-5 channels contains a conserved protein kinase C (PKC) phosphorylation site, suggesting that phosphorylation may reg...