Functional domains within the degenerin/epithelial sodium channel (Deg/ENaC) superfamily of ion channels

作     者：Benos, DJ Stanton, BA 

作者机构：Univ Alabama Birmingham Dept Physiol & Biophys Birmingham AL 35294 USA Dartmouth Med Sch Dept Physiol Hanover NH 03755 USA 

出 版 物：《JOURNAL OF PHYSIOLOGY-LONDON》 (生理学杂志)

年 卷 期：1999年第520卷第3期

页      面：631-644页

核心收录：

学科分类：0710[理学-生物学] 1001[医学-基础医学(可授医学、理学学位)] 07[理学] 071003[理学-生理学] 

基　　金：NIDDK NIH HHS [R01 DK034533  R01 DK037206  R56 DK037206  DK37206  DK56095  DK34533] Funding Source: Medline 

主　　题：氨基酸序列/遗传学 细胞质/代谢 离子通道/遗传学 离子通道/生理学 分子序列数据 神经组织蛋白质类/遗传学 神经组织蛋白质类/生理学 钠通道/遗传学 钠通道/生理学 动物 

摘      要：Application of recombinant DNA technology and electrophysiology to the study of amiloride-sensitive Naf channels has resulted in an enormous increase in the understanding of the structure-function relationships of these channels. Moreover, this knowledge has permitted the elucidation of the physiological roles of these ion channels in cellular processes as diverse as transepithelial salt and water movement, taste perception, volume regulation, nociception, neuronal function, mechanosensation, and even defaecation. Although members of this ever-growing superfamily of ion channels (the Deg/ENaC superfamily) share little amino acid identity, they are all organized similarly, namely, two short N- and C-termini, two short membrane-spanning segments, and a very large extracellular loop domain. In this brief Topical Review, we discuss the structural features of each domain of this Deg/ENaC superfamily and, using ENaC as a model, show how each domain relates to overall channel function.