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rdf:type | |
lifeskim:mentions | |
pubmed:dateCreated |
1984-7-11
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pubmed:abstractText |
Our experiments have delineated the flow of information in the cyclic nucleotide cascade of vision of ROS. A single, photoexcited rhodopsin molecule activates several hundred phosphodiesterase molecules in two stages. First, photoexcited rhodopsin (R*) interacts with transducin (T), a peripheral membrane protein consisting of alpha- (39 kD), beta- (36 kD), and gamma- (approximately 10 kD) subunits. R* catalyzes the exchange of GTP for GDP bound to the subunit of transducin. About 500 T alpha- GTPs are produced per photoexcited rhodopsin at low light levels. T alpha-GTP, released from the beta- and gamma-subunits of transducin, then interacts with the phosphodiesterase to relieve the inhibitory constraint imposed by its gamma-subunit. Hydrolysis of GTP bound to T alpha serves to restore the system to the dark state. Transducin is the amplified signal carrier in this light-triggered cascade. The formation of hundreds of T alpha- GTPs is likely to be the first stage of amplification in visual excitation. The photoactivation of the phosphodiesterase in ROS closely resembles the activation of adenylate cyclase in hormone-sensitive cells. Our cholera toxin labeling studies have shown that transducin is akin to the signal-coupling G protein of the adenylate cyclase system. Cholera toxin specifically ADP- ribosylates and inactivates the GTPase activity of T alpha, just as it does with Gs. The action of pertussis toxin on ROS further underscores the homology of the photoreceptor and hormone-responsive systems. It seems likely that transducin, the stimulatory G protein, and the inhibitory G protein are members of the same family of signal-amplifying proteins. The study of the cyclic nucleotide cascade of vision is proving to be rewarding in affording a view of a recurring motif of signal amplification in nature in addition to providing insight into the mechanism of vision.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/3',5'-Cyclic-GMP Phosphodiesterases,
http://linkedlifedata.com/resource/pubmed/chemical/Guanosine Diphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Guanosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Retinal Pigments,
http://linkedlifedata.com/resource/pubmed/chemical/Rhodopsin,
http://linkedlifedata.com/resource/pubmed/chemical/Transducin,
http://linkedlifedata.com/resource/pubmed/chemical/Trypsin
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pubmed:status |
MEDLINE
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pubmed:issn |
0091-7451
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
48 Pt 2
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
841-52
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:6327179-3',5'-Cyclic-GMP Phosphodiesterases,
pubmed-meshheading:6327179-Animals,
pubmed-meshheading:6327179-Enzyme Activation,
pubmed-meshheading:6327179-Guanosine Diphosphate,
pubmed-meshheading:6327179-Guanosine Triphosphate,
pubmed-meshheading:6327179-Light,
pubmed-meshheading:6327179-Macromolecular Substances,
pubmed-meshheading:6327179-Membrane Proteins,
pubmed-meshheading:6327179-Photolysis,
pubmed-meshheading:6327179-Photoreceptor Cells,
pubmed-meshheading:6327179-Retinal Pigments,
pubmed-meshheading:6327179-Rhodopsin,
pubmed-meshheading:6327179-Transducin,
pubmed-meshheading:6327179-Trypsin,
pubmed-meshheading:6327179-Vision, Ocular
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pubmed:year |
1983
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pubmed:articleTitle |
Transducin and the cyclic GMP phosphodiesterase: amplifier proteins in vision.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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