Publication Date:
1998-10-02
Description:
Heterotrimeric guanosine 5'-triphosphate (GTP)-binding proteins (G proteins) are deactivated by hydrolysis of the GTP that they bind when activated by transmembrane receptors. Transducin, the G protein that relays visual excitation from rhodopsin to the cyclic guanosine 3',5'-monophosphate phosphodiesterase (PDE) in retinal photoreceptors, must be deactivated for the light response to recover. A point mutation in the gamma subunit of PDE impaired transducin-PDE interactions and slowed the recovery rate of the flash response in transgenic mouse rods. These results indicate that the normal deactivation of transducin in vivo requires the G protein to interact with its target enzyme.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tsang, S H -- Burns, M E -- Calvert, P D -- Gouras, P -- Baylor, D A -- Goff, S P -- Arshavsky, V Y -- EY05750/EY/NEI NIH HHS/ -- EY10336/EY/NEI NIH HHS/ -- T32 EY07105/EY/NEI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1998 Oct 2;282(5386):117-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Edward S. Harkness Eye Institute and Department of Biochemistry and Molecular Biophysics, Columbia University, College of Physicians and Surgeons, New York, NY 10032, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9756475" target="_blank"〉PubMed〈/a〉
Keywords:
3',5'-Cyclic-GMP Phosphodiesterases/genetics/*metabolism
;
Animals
;
Cyclic Nucleotide Phosphodiesterases, Type 6
;
Electroretinography
;
Enzyme Activation
;
Female
;
Guanosine 5'-O-(3-Thiotriphosphate)/pharmacology
;
Guanosine Triphosphate/metabolism
;
Hydrolysis
;
Light
;
Male
;
Mice
;
Mice, Knockout
;
Mice, Transgenic
;
Point Mutation
;
Retina/cytology/physiology
;
Retinal Degeneration
;
Rod Cell Outer Segment/*metabolism
;
Transducin/*metabolism
;
Transgenes
;
*Vision, Ocular
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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