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Calmodulin acts as a state-dependent switch to control a cardiac potassium channel opening
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- Kang, Po Wei (författare)
- Washington Univ, Dept Biomed Engn, Ctr Invest Membrane Excitabil Disorders & Cardiac, St Louis, MO 63130 USA.;Washington Univ, Arrhythmia Ctr, St Louis, MO 63130 USA.
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- Westerlund, Annie M. (författare)
- KTH,Biofysik,Science for Life Laboratory, SciLifeLab
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- Shi, Jingyi (författare)
- Washington Univ, Dept Biomed Engn, Ctr Invest Membrane Excitabil Disorders & Cardiac, St Louis, MO 63130 USA.;Washington Univ, Arrhythmia Ctr, St Louis, MO 63130 USA.
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- Washington Univ, Dept Biomed Engn, Ctr Invest Membrane Excitabil Disorders & Cardiac, St Louis, MO 63130 USA;Washington Univ, Arrhythmia Ctr, St Louis, MO 63130 USA. Biofysik (creator_code:org_t)
- American Association for the Advancement of Science (AAAS), 2020
- 2020
- Engelska.
- Ingår i: Science Advances. - : American Association for the Advancement of Science (AAAS). - 2375-2548. ; 6:50
- Tidskriftsartikel (refereegranskat)
Abstract
Ämnesord
Stäng
- Calmodulin (CaM) and phosphatidylinositol 4,5-bisphosphate (PIP2) are potent regulators of the voltage-gated potassium channel KCNQ1 (K(v)7.1), which conducts the cardiac I-Ks current. Although cryo-electron microscopy structures revealed intricate interactions between the KCNQ1 voltage-sensing domain (VSD), CaM, and PIP2, the functional consequences of these interactions remain unknown. Here, we show that CaM-VSD interactions act as a state-dependent switch to control KCNQ1 pore opening. Combined electrophysiology and molecular dynamics network analysis suggest that VSD transition into the fully activated state allows PIP 2 to compete with CaM for binding to VSD. This leads to conformational changes that alter VSD-pore coupling to stabilize open states. We identify a motif in the KCNQ1 cytosolic domain, which works downstream of CaM-VSD interactions to facilitate the conformational change. Our findings suggest a gating mechanism that integrates PIP2 and CaM in KCNQ1 voltage-dependent activation, yielding insights into how KCNQ1 gains the phenotypes critical for its physiological function.
Ämnesord
- NATURVETENSKAP -- Biologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences (hsv//eng)
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