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

@article{Tobelaim2017CompetitionOC,
  title={Competition of calcified calmodulin N lobe and PIP2 to an LQT mutation site in Kv7.1 channel.},
  author={William Sam Tobelaim and Meidan Dvir and Guy Lebel and M. C. Cui and Tal Buki and Asher Peretz and Milit Marom and Yoni Haitin and Diomedes E. Logothetis and Joel Alan Hirsch and Bernard Attali},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2017},
  volume={114 5},
  pages={E869-E878}
}
Voltage-gated potassium 7.1 (Kv7.1) channel and KCNE1 protein coassembly forms the slow potassium current IKS that repolarizes the cardiac action potential. The physiological importance of the IKS 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… CONTINUE READING
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Structural basis of a Kv7.1 potassium channel gating module: Studies of the intracellular c-terminal domain in complex with calmodulin

  • D Sachyani
  • Structure
  • 2014
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