| First Author | Tsang SH | Year | 1998 |
| Journal | Science | Volume | 282 |
| Issue | 5386 | Pages | 117-21 |
| PubMed ID | 9756475 | Mgi Jnum | J:108194 |
| Mgi Id | MGI:3623195 | Doi | 10.1126/science.282.5386.117 |
| Citation | Tsang SH, et al. (1998) Role for the target enzyme in deactivation of photoreceptor G protein in vivo. Science 282(5386):117-21 |
| abstractText | 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. |
