The cGMP-gated channel of photoreceptor cells: Its structural properties and role in phototransduction
Identifieur interne : 000C55 ( Main/Exploration ); précédent : 000C54; suivant : 000C56The cGMP-gated channel of photoreceptor cells: Its structural properties and role in phototransduction
Auteurs : Robert S. Molday [Canada] ; Yi-Te Hsu [Canada]Source :
- Behavioral and Brain Sciences [ 0140-525X ] ; 1995-09.
Abstract
The cyclic GMP-gated channel responds to changes in free intracellular cGMP, and as a result, it plays a central role in the phototransduction process in rod and cone photoreceptor cells. Recent biochemical, immunochemical, and molecular biology studies indicate that this channel consists of a complex of two distinct subunits and one or more associated proteins. Primary structural analysis indicates that the a and (3 subunits contain a cGMP-binding domain, an even number of membrane-spanning segments, a voltage sensor motif and a pore region. The latter two features are found in voltage-gated channels and suggest that these two classes of channels have evolved from the same ancestral channel protein. A working model for the membrane topography of the channel subunits is proposed based on immunogold labeling studies and sequence analysis. Recent studies also indicate that calmodulin binds to the 240 kDa protein of the channel complex and modulates the sensitivity of the channel for cGMP in a Ca2+-dependent manner. The molecular properties of the channel complex and the possible role of Ca2+-calmodulin modulation of the channel during photoactivation and photorecovery are discussed in relation to the current mechanism of phototransduction in photoreceptor cells
Url:
DOI: 10.1017/S0140525X00039200
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="441">441</biblScope><biblScope unit="page" to="451">451</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">The cyclic GMP-gated channel responds to changes in free intracellular cGMP, and as a result, it plays a central role in the phototransduction process in rod and cone photoreceptor cells. Recent biochemical, immunochemical, and molecular biology studies indicate that this channel consists of a complex of two distinct subunits and one or more associated proteins. Primary structural analysis indicates that the a and (3 subunits contain a cGMP-binding domain, an even number of membrane-spanning segments, a voltage sensor motif and a pore region. The latter two features are found in voltage-gated channels and suggest that these two classes of channels have evolved from the same ancestral channel protein. A working model for the membrane topography of the channel subunits is proposed based on immunogold labeling studies and sequence analysis. Recent studies also indicate that calmodulin binds to the 240 kDa protein of the channel complex and modulates the sensitivity of the channel for cGMP in a Ca2+-dependent manner. The molecular properties of the channel complex and the possible role of Ca2+-calmodulin modulation of the channel during photoactivation and photorecovery are discussed in relation to the current mechanism of phototransduction in photoreceptor cells</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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