PIP2 regulation of KCNQ channels: biophysical and molecular mechanisms for lipid modulation of voltage-dependent gating

被引：100

作者：

Zaydman, Mark A. ^{[1
]}

Cui, Jianmin ^{[1
]}

机构：

[1] Washington Univ, Cardiac Bioelect & Arrhythmia Ctr, Ctr Invest Membrane Excitabil Dis, Dept Biomed Engn, St Louis, MO 63130 USA

来源：

FRONTIERS IN PHYSIOLOGY | 2014年 / 5卷

关键词：

PIP2; voltage-gating; lipid modulations; ion channel; KCNQ; GATED POTASSIUM CHANNELS; K+ CHANNEL; PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE; CRYSTAL-STRUCTURE; ION CHANNELS; I-KS; FUNCTIONAL RECONSTITUTION; STRUCTURAL BASIS; CHARGE MOVEMENT; SENSOR-DOMAIN;

D O I：

10.3389/fphys.2014.00195

中图分类号：

Q4 [生理学];

学科分类号：

071003 ;

摘要：

Voltage-gated potassium (Kv) channels contain voltage-sensing (VSD) and pore-gate (PGD) structural domains. During voltage-dependent gating, conformational changes in the two domains are coupled giving rise to voltage-dependent opening of the channel. In addition to membrane voltage, KCNQ (Kv7) channel opening requires the membrane lipid phosphatidylinositol 4,5-bisphosphate (PIP2). Recent studies suggest that PIP2 serves as a cofactor to mediate VSD-PGD coupling in KCNQ1 channels. In this review, we put these findings in the context of the current understanding of voltage-dependent gating, lipid modulation of Kv channel activation, and PIP2-regulation of KCNQ channels. We suggest that lipid-mediated coupling of functional domains is a common mechanism among KCNQ channels that may be applicable to other Kv channels and membrane proteins.

引用

页数：11

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