Linked Life Data

9804777

Source:http://linkedlifedata.com/resource/pubmed/id/9804777

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pubmed-article:9804777pubmed:abstractTextBNC1 is a mammalian neuronal cation channel in the novel DEG/ENaC ion channel family. BNC1 channels are transiently activated by extracellular protons and are constitutively activated by insertion of large residues, such as valine, in place of Gly-430; residue 430 is a site where analogous mutations in some Caenorhabditis elegans family members cause a swelling neurodegeneration. Mutation of Gly-430 to a small amino acid, cysteine, neither generated constitutive currents nor allowed modification of this residue by sulfhydryl-reactive methanethiosulfonate (MTS) compounds. However, when protons activated the channel, Cys-430 became accessible to extracellular MTS reagents, which modified Cys-430 to generate constitutive currents. Fluorescent MTS reagents also labeled Cys-430 in activated channels. These data indicate that protons induce a reversible conformational change that activates BNC1 thereby exposing residue 430 to the extracellular solution. Once Cys-430 is modified with a large chemical group, the channel is prevented from relaxing back to the inactive state. These results link ligand-dependent activation and activation by mutations that cause neurodegeneration.lld:pubmed
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pubmed-article:9804777pubmed:articleTitleProtons activate brain Na+ channel 1 by inducing a conformational change that exposes a residue associated with neurodegeneration.lld:pubmed
pubmed-article:9804777pubmed:affiliationHoward Hughes Medical Institute, Departments of Internal Medicine and Physiology and Biophysics, University of Iowa College of Medicine, Iowa City, Iowa 52242, USA.lld:pubmed
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pubmed-article:9804777pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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