title: Insight into DEG/ENaC channel gating from genetics and structure.
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.
authors.affiliation: Department of Molecular and Cellular Physiology, Stanford University, Stanford, California, USA. aeastwood@stanford.edu
authors.forename: Amy L
authors.initials: AL
authors.lastname: Eastwood
authors.forename: Miriam B
authors.initials: MB
authors.lastname: Goodman
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D017173:Caenorhabditis elegans / Q000235:genetics* / Q000502:physiology*; D029742:Caenorhabditis elegans Proteins / Q000737:chemistry / Q000235:genetics* / Q000502:physiology*; D053503:Epithelial Sodium Channels / Q000737:chemistry / Q000235:genetics / Q000502:physiology; D015640:Ion Channel Gating / Q000502:physiology; D008565:Membrane Proteins / Q000737:chemistry / Q000235:genetics* / Q000502:physiology*; D008969:Molecular Sequence Data; D010146:Pain / Q000503:physiopathology; D014110:Touch / Q000502:physiology
chemical_list: D029742:Caenorhabditis elegans Proteins; C094927:Deg-1 protein, C elegans; D053503:Epithelial Sodium Channels; D008565:Membrane Proteins