Insight into DEG/ENaC Channel Gating from Genetics and Structure

Amy L. Eastwood, Miriam B. Goodman

Abstract

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.

Footnotes

  • While this review was in press, new ASIC1a structures were published that provide insight into the psalmotoxin-1 binding site and the conformation of putative open channels (5a, 18a). Consistent with the ideas presented here, Baconguis and Gouaux (5a) note that the lower palm and pore domains are wider in the open structure than they are in the desensitized structure.

  • No conflicts of interest, financial or otherwise, are declared by the author(s).

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