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Po Wei Kang on Muck Rack

Po Wei Kang

As seen in: Science Magazine, BioRxiv
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Articles

Arrhythmia-associated Calmodulin Variants Interact with KCNQ1 to Confer Aberrant Membrane Trafficking and Function

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By Po Wei Kang, Lucy Woodbury, Paweorn Angsutararux, Namit Sambare
| BioRxiv
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Calmodulin acts as a state-dependent switch to control a cardiac potassium channel opening

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By Annie M. Westerlund, Jingyi Shi, Kelli White, Po Wei Kang
| Science Magazine Verified
Abstract Calmodulin (CaM) and phosphatidylinositol 4,5-bisphosphate (PIP2) are potent regulators of the voltage-gated potassium channel KCNQ1 (KV7.1), which conducts the cardiac IKs 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.
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