Further insight into the structural and regulatory properties of the cGMP-gated channel
Identifieur interne : 000D12 ( Main/Exploration ); précédent : 000D11; suivant : 000D13Further insight into the structural and regulatory properties of the cGMP-gated channel
Auteurs : Robert S. Molday [Canada] ; Yi-Te Hsu [Canada]Source :
- Behavioral and Brain Sciences [ 0140-525X ] ; 1995-09.
Abstract
Recent studies from several different laboratories have provided further insight into structure-function relationships of cyclic nucleotide-gated channel and in particular the cCMPgated channel of rod photoreceptors. Site-directed mutagenesis and rod-olfactory chimeria constructs have defined important amino acids and peptide segments of the channel that are important in ion blockage, ligand specificity, and gating properties. Molecular cloning studies have indicated that cyclic nucleotide-gated channels consist of two subunits that are required to reproduce the properties of the native channels. Biochemical analysis of the cGMP-gated channel of rodcells have indicated that the 240 kDa protein that co-purifies with the 63 kDa channel subunit contains both the previously cloned second subunit of the channel and a glutamic acid-rich protein. The regulatory properties of the cGMP-gated channel from rod cells has also been studied in more detail. Studies indicate that the beta subunit of the cGMP-gated channel of rod cells contains the binding site for calmodulin. Interaction of calmodulin with the channel alters the apparent affinity of the channel for cGMP in all in vitro systems that have been studied. The significance of these recent studies are discussed in relation to the commentaries on the target article.
Url:
DOI: 10.1017/S0140525X00039571
Affiliations:
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Molday</name><affiliation wicri:level="4"><country wicri:rule="url">Canada</country><wicri:regionArea>Department of Biochemistry and Molecular Biology, University of British Columbia, Vancouver, B.C.</wicri:regionArea><orgName type="university">Université de la Colombie-Britannique</orgName><placeName><settlement type="city">Vancouver</settlement><region type="state">Colombie-Britannique </region></placeName></affiliation><affiliation wicri:level="1"><country wicri:rule="url">Canada</country></affiliation></author><author><name sortKey="Hsu, Yi Te" sort="Hsu, Yi Te" uniqKey="Hsu Y" first="Yi-Te" last="Hsu">Yi-Te Hsu</name><affiliation wicri:level="4"><country>Canada</country><wicri:regionArea>Department of Biochemistry and Molecular Biology, University of British Columbia, Vancouver, B.C.</wicri:regionArea><orgName type="university">Université de la Colombie-Britannique</orgName><placeName><settlement type="city">Vancouver</settlement><region type="state">Colombie-Britannique </region></placeName></affiliation></author></analytic><monogr></monogr><series><title level="j">Behavioral and Brain Sciences</title><title level="j" type="abbrev">Behav Brain Sci</title><idno type="ISSN">0140-525X</idno><idno type="eISSN">1469-1825</idno><imprint><publisher>Cambridge University Press</publisher><pubPlace>Cambridge, UK</pubPlace><date type="published" when="1995-09">1995-09</date><biblScope unit="volume">18</biblScope><biblScope unit="issue">3</biblScope><biblScope unit="page" from="500">500</biblScope><biblScope unit="page" to="501">501</biblScope></imprint><idno type="ISSN">0140-525X</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0140-525X</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract">Recent studies from several different laboratories have provided further insight into structure-function relationships of cyclic nucleotide-gated channel and in particular the cCMPgated channel of rod photoreceptors. Site-directed mutagenesis and rod-olfactory chimeria constructs have defined important amino acids and peptide segments of the channel that are important in ion blockage, ligand specificity, and gating properties. Molecular cloning studies have indicated that cyclic nucleotide-gated channels consist of two subunits that are required to reproduce the properties of the native channels. Biochemical analysis of the cGMP-gated channel of rodcells have indicated that the 240 kDa protein that co-purifies with the 63 kDa channel subunit contains both the previously cloned second subunit of the channel and a glutamic acid-rich protein. The regulatory properties of the cGMP-gated channel from rod cells has also been studied in more detail. Studies indicate that the beta subunit of the cGMP-gated channel of rod cells contains the binding site for calmodulin. Interaction of calmodulin with the channel alters the apparent affinity of the channel for cGMP in all in vitro systems that have been studied. The significance of these recent studies are discussed in relation to the commentaries on the target article.</div></front></TEI><affiliations><list><country><li>Canada</li></country><region><li>Colombie-Britannique </li></region><settlement><li>Vancouver</li></settlement><orgName><li>Université de la Colombie-Britannique</li></orgName></list><tree><country name="Canada"><region name="Colombie-Britannique "><name sortKey="Molday, Robert S" sort="Molday, Robert S" uniqKey="Molday R" first="Robert S." last="Molday">Robert S. Molday</name></region><name sortKey="Hsu, Yi Te" sort="Hsu, Yi Te" uniqKey="Hsu Y" first="Yi-Te" last="Hsu">Yi-Te Hsu</name><name sortKey="Molday, Robert S" sort="Molday, Robert S" uniqKey="Molday R" first="Robert S." last="Molday">Robert S. 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