The voltage sensor domain (VSD) has long been studied as a unique domain intrinsic to voltage-gated ion channels (VGICs). Within VGICs, the VSD is tightly coupled to the pore-gate domain (PGD) in diverse ways suitable for its specific function in each physiological context, including action potential generation, muscle contraction and relaxation, hormone and neurotransmitter secretion, and cardiac pacemaking. However, some VSD-containing proteins lack a PGD. Voltage-sensing phosphatase contains a cytoplasmic phosphoinositide phosphatase with similarity to phosphatase and tensin homolog (PTEN). Hv1, a voltage-gated proton channel, also lacks a PGD. Within Hv1, the VSD operates as a voltage sensor, gate, and pore for both proton sensing and permeation. Hv1 has a C-terminal coiled coil that mediates dimerization for cooperative gating. Recent progress in the structural biology of VGICs and VSD proteins provides insights into the principles of VSD coupling conserved among these proteins as well as the hierarchy of protein organization for voltage-evoked cell signaling.

中文翻译：

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在电压诱发的细胞信号中耦合到电压传感器的分子机制。

长期以来，电压传感器域 (VSD) 一直被研究为电压门控离子通道 (VGIC) 固有的独特域。在 VGIC 中，VSD 以适合其在每个生理环境中的特定功能的多种方式与孔门域 (PGD) 紧密耦合，包括动作电位生成、肌肉收缩和放松、激素和神经递质分泌以及心脏起搏。然而，一些含有 VSD 的蛋白质缺乏 PGD。电压感应磷酸酶包含与磷酸酶和张力蛋白同源物 (PTEN) 相似的细胞质磷酸肌醇磷酸酶。Hv1 是一种电压门控质子通道，也没有 PGD。在 Hv1 中，VSD 作为电压传感器、栅极和孔用于质子传感和渗透。Hv1 有一个 C 端盘绕线圈，介导协同门控的二聚化。