Role for the target enzyme in deactivation of photoreceptor G protein in vivo

Stephen H. Tsang, Marie E Burns, Peter D. Calvert, Peter Gouras, Denis A. Baylor, Stephen P. Goff, Vadim Y. Arshavsky

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Abstract

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 γ 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.

Original languageEnglish (US)
Pages (from-to)117-121
Number of pages5
JournalScience
Volume282
Issue number5386
DOIs
StatePublished - Oct 2 1998
Externally publishedYes

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Cite this

Tsang, S. H., Burns, M. E., Calvert, P. D., Gouras, P., Baylor, D. A., Goff, S. P., & Arshavsky, V. Y. (1998). Role for the target enzyme in deactivation of photoreceptor G protein in vivo. Science, 282(5386), 117-121. https://doi.org/10.1126/science.282.5386.117