Renal-Electrolyte Division, Department of Medicine, University of Pittsburgh, Pittsburgh, Pennsylvania 15261, USA.
Am J Physiol Renal Physiol. 2011 Oct;301(4):F684-96. doi: 10.1152/ajprenal.00259.2011. Epub 2011 Jul 13.
Our understanding of epithelial Na(+) channel (ENaC) structure and function has been profoundly impacted by the resolved structure of the homologous acid-sensing ion channel 1 (ASIC1). The structure of the extracellular and pore regions provide insight into channel assembly, processing, and the ability of these channels to sense the external environment. The absence of intracellular structures precludes insight into important interactions with intracellular factors that regulate trafficking and function. The primary sequences of ASIC1 and ENaC subunits are well conserved within the regions that are within or in close proximity to the plasma membrane, but poorly conserved in peripheral domains that may functionally differentiate family members. This review examines functional data, including ion selectivity, gating, and amiloride block, in light of the resolved ASIC1 structure.
我们对上皮钠离子通道（ENaC）结构和功能的理解受到已解析的同源酸感应离子通道 1（ASIC1）结构的深刻影响。细胞外和孔区的结构提供了对通道组装、加工以及这些通道感知外部环境的能力的深入了解。缺乏细胞内结构使得无法深入了解与调节运输和功能的细胞内因素的重要相互作用。ASIC1 和 ENaC 亚基的一级序列在位于或靠近质膜的区域内具有很好的保守性，但在可能在功能上区分家族成员的外围结构域中保守性较差。本综述根据已解析的 ASIC1 结构，检查了功能数据，包括离子选择性、门控和阿米洛利阻断。
