Role for the target enzyme in deactivation of photoreceptor G protein in vivo
Science, 1998•science.org
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 …
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 …
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.
AAAS