Ca2+-Calmodulin and PIP2 interactions at the proximal C-terminus of Kv7 channels

William S. Tobelaim, Meidan Dvir, Guy Lebel, Meng Cui, Tal Buki, Asher Peretz, Milit Marom, Yoni Haitin, Diomedes E. Logothetis, Joel A. Hirsch, Bernard Attali

Research output: Contribution to journalArticlepeer-review


In the heart, co-assembly of Kv7.1 with KCNE1 produces the slow IKS potassium current, which repolarizes the cardiac action potential and mutations in human Kv7.1 and KCNE1 genes cause cardiac arrhythmias. The proximal Kv7.1 C-terminus binds calmodulin (CaM) and phosphatidylinositol-4,5-bisphosphate (PIP2) and recently we revealed the competition of PIP2 with the calcified CaM N-lobe to a previously unidentified site in Kv7.1 helix B, also known to harbor a LQT mutation. Data indicated that PIP2 and Ca2+-CaM perform the same function on IKS channel gating to stabilize the channel open state. Here we show that similar features were observed for Kv7.1 currents expressed alone. We also find that conservation of homologous residues in helix B of other Kv7 subtypes confer similar competition of Ca2+-CaM with PIP2 binding to their proximal C-termini and suggest that PIP2-CaM interactions converge to Kv7 helix B to modulates channel activity in a Kv7 subtype-dependent manner.

Original languageEnglish
Pages (from-to)686-695
Number of pages10
Issue number6
StatePublished - 2 Nov 2017


  • KCNQ
  • Kv7
  • PIP2
  • Potassium channel
  • calmodulin

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry


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