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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Schmitt, Nicole Eckey, Karina Strutz-seebohm, Nathalie Pott, Lutz Seebohm, Guiscard Wrobel, Eva |
| Description | Author Affiliation: Eckey K ( From the Department of Biochemistry I-Cation Channel Group, the International Graduate School of Neuroscience, the Ruhr University Bochum Research School, and.); Wrobel E ( the IfGH-Myocellular Electrophysiology, Department of Cardiovascular Medicine, University Hospital of Münster, 48149 Münster, Germany, and.); Strutz-Seebohm N ( the IfGH-Myocellular Electrophysiology, Department of Cardiovascular Medicine, University Hospital of Münster, 48149 Münster, Germany, and.); Pott L ( the Institute of Physiology, Ruhr University Bochum, 44801 Bochum, Germany.); Schmitt N ( the Danish National Research Foundation Centre for Cardiac Arrhythmia, University of Copenhagen, 1165 Copenhagen, Denmark.); Seebohm G ( the International Graduate School of Neuroscience, the Ruhr University Bochum Research School, and the IfGH-Myocellular Electrophysiology, Department of Cardiovascular Medicine, University Hospital of Münster, 48149 Münster, Germany, and guiscard.seebohm@ukmuenster.de.) |
| Abstract | Kv7.1 to Kv7.5 -subunits belong to the family of voltage-gated potassium channels (Kv). Assembled with the ß-subunit KCNE1, Kv7.1 conducts the slowly activating potassium current IKs, which is one of the major currents underlying repolarization of the cardiac action potential. A known regulator of Kv7 channels is the lipid phosphatidylinositol 4,5-bisphosphate (PIP2). PIP2 increases the macroscopic current amplitude by stabilizing the open conformation of 7.1/KCNE1 channels. However, knowledge about the exact nature of the interaction is incomplete. The aim of this study was the identification of the amino acids responsible for the interaction between Kv7.1 and PIP2. We generated 13 charge neutralizing point mutations at the intracellular membrane border and characterized them electrophysiologically in complex with KCNE1 under the influence of diC8-PIP2. Electrophysiological analysis of corresponding long QT syndrome mutants suggested impaired PIP2 regulation as the cause for channel dysfunction. To clarify the underlying structural mechanism of PIP2 binding, molecular dynamics simulations of Kv7.1/KCNE1 complexes containing two PIP2 molecules in each subunit at specific sites were performed. Here, we identified a subset of nine residues participating in the interaction of PIP2 and Kv7.1/KCNE1. These residues may form at least two binding pockets per subunit, leading to the stabilization of channel conformations upon PIP2 binding. |
| ISSN | 00219258 |
| e-ISSN | 1083351X |
| Journal | Journal of Biological Chemistry |
| Issue Number | 33 |
| Volume Number | 289 |
| Language | English |
| Publisher | American Society for Biochemistry and Molecular Biology (United States) |
| Publisher Date | 2014-08-15 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | KCNQ1 Potassium Channel Metabolism Phosphatidylinositol 4,5-Diphosphate Action Potentials Physiology Amino Acid Substitution Animals Binding Sites Chemistry Genetics Point Mutation Protein Binding Xenopus Laevis Research Support, Non-U.S. Gov't Biochemistry Molecular Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
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