The extracellular loop of pendrin and prestin modulates their voltage-sensing property
The extracellular loop of pendrin and prestin modulates their voltage-sensing property
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DOI：
10.1074/jbc.ra118.001831
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发表时间：
2018-06-29
影响因子：
4.8
通讯作者：
Homma, Kazuaki
中科院分区：
文献类型：
--
作者：
Kuwabara, Makoto F.;Wasano, Koichiro;Homma, Kazuaki
Pendrin和普雷斯廷属于溶质载体26（SLC 26）家族的阴离子转运蛋白。普雷斯廷在SLC 26家族成员中是独特的，因为它显示电压驱动的运动活动（电运动性）和表现为非线性细胞膜电容（非线性电容（NLC））的并发门控电流。虽然SLC26蛋白的阴离子转运机制已开始阐明，电迁移的分子机制，这被认为是从祖先的离子转运机制，仍然在很大程度上难以捉摸。在这里，我们表明，pendrin也表现出大的NLC和收费残基存在于pendrin和普雷斯廷的细胞外环之一发挥重要作用，在设置的电压工作点的NLC。我们的研究结果表明，负责感知电压的分子机制是不是唯一的普雷斯廷之间的SLC26家族的成员，这种电压传感机制的工作独立的阴离子转运机制。
Pendrin and prestin belong to the solute carrier 26 (SLC26) family of anion transporters. Prestin is unique among the SLC26 family members in that it displays voltage-driven motor activity (electromotility) and concurrent gating currents that manifest as nonlinear cell membrane electrical capacitance (nonlinear capacitance (NLC)). Although the anion transport mechanism of the SLC26 proteins has begun to be elucidated, the molecular mechanism of electromotility, which is thought to have evolved from an ancestral ion transport mechanism, still remains largely elusive. Here, we demonstrate that pendrin also exhibits large NLC and that charged residues present in one of the extracellular loops of pendrin and prestin play significant roles in setting the voltage-operating points of NLC. Our results suggest that the molecular mechanism responsible for sensing voltage is not unique to prestin among the members of the SLC26 family and that this voltage-sensing mechanism works independently of the anion transport mechanism.