Insight into DEG/ENaC Channel Gating from Genetics and Structure

被引：55
作者：
Eastwood, Amy L. [1 ]
Goodman, Miriam B. [1 ]
机构：
[1] Stanford Univ, Dept Mol & Cellular Physiol, Stanford, CA 94305 USA
来源：
PHYSIOLOGY | 2012年 / 27卷 / 05期
关键词：
EPITHELIAL SODIUM-CHANNEL; ACID-SENSING ION-CHANNEL-1; ION-CHANNEL; EXTRACELLULAR DOMAIN; NA+ CHANNEL; PORE REGION; TRANSMEMBRANE DOMAIN; SELECTIVITY FILTER; CRYSTAL-STRUCTURE; MEC-4;
D O I：
10.1152/physiol.00006.2012
中图分类号：
Q4 [生理学];
学科分类号：
071003 ;
摘要：
The founding members of the superfamily of DEG/ENaC ion channel proteins are C. elegans proteins that form mechanosensitive channels in touch and pain receptors. For more than a decade, the research community has used mutagenesis to identify motifs that regulate gating. This review integrates insight derived from unbiased in vivo mutagenesis screens with recent crystal structures to develop new models for activation of mechanically gated DEGs.
引用
收藏
页码：282 / 290
页数：9
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