PIP2 activation of the cardiac IKs potassium channel
Lu Zhao, Xianjin Xu, Chenxi Cui, Rui Duan, Ali A. Kermani, Jingyi Shi, Lu Han, Ji Sun, Xiaoqin Zou, Jianmin Cui · 2026
Read PIP2 activation of the cardiac IKs potassium channel by Lu Zhao, Xianjin Xu, Chenxi Cui, Rui Duan, Ali A. Kermani, Jingyi Shi, Lu Han, Ji Sun, Xiaoqin Zou, Jianmin Cui (2026) in the Tower of Babel, a free online library of public-domain works preserved in clean, searchable text. No sign-up. The full text is served as a plain-text file at a predictable URL, where text is present: https://antarctic-labs.com/tower-of-babel/PMC13402814.txt.
Description
Lu Zhao and co-authors untangle how the lipid PIP2 switches on the cardiac IKs potassium channel, the current that times each heartbeat reset. The channel pairs the pore protein KCNQ1 with its partner KCNE1 and cannot open without PIP2. Two PIP2 molecules bind at distinct spots: one beside the voltage sensor, one at the sensor-pore interface.
Each does a separate job. The sensor-side lipid lets the channel bend from its intermediate shape into the straight, fully open form unique to IKs. The interface lipid, in turn, locks sensor to pore and holds that form steady. Guided by the split, the team built compound CA1, which targets the sensor-side pocket and tunes IKs without touching plain KCNQ1 channels. They offer CA1 as a conceptual path toward safer antiarrhythmic drugs aimed at one channel flavor only.
Catalog record
| CREATOR | Lu Zhao, Xianjin Xu, Chenxi Cui, Rui Duan, Ali A. Kermani, Jingyi Shi, Lu Han, Ji Sun, Xiaoqin Zou, Jianmin Cui |
|---|---|
| YEAR | 2026 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 72545 |
| LICENSE | https://creativecommons.org/licenses/by/4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |