Competition of calcified calmodulin N lobe and PIP2 to an LQT mutation site in Kv7.1 channel.

ABSTRACT: Voltage-gated potassium 7.1 (Kv7.1) channel and KCNE1 protein coassembly forms the slow potassium current I_KS that repolarizes the cardiac action potential. The physiological importance of the I_KS channel is underscored by the existence of mutations in human Kv7.1 and KCNE1 genes, which cause cardiac arrhythmias, such as the long-QT syndrome (LQT) and atrial fibrillation. The proximal Kv7.1 C terminus (CT) binds calmodulin (CaM) and phosphatidylinositol-4,5-bisphosphate (PIP₂), but the role of CaM in channel function is still unclear, and its possible interaction with PIP₂ is unknown. Our recent crystallographic study showed that CaM embraces helices A and B with the apo C lobe and calcified N lobe, respectively. Here, we reveal the competition o

SUBMITTER: Tobelaim WS 

PROVIDER: S-EPMC5293103 | biostudies-literature | 2017 Jan

REPOSITORIES: biostudies-literature