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Science 2 October 1998:
Vol. 282. no. 5386, pp. 117 - 121
DOI: 10.1126/science.282.5386.117
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Reports

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 dagger

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.

S. H. Tsang, Edward S. Harkness Eye Institute and Department of Biochemistry and Molecular Biophysics, Columbia University, College of Physicians and Surgeons, New York, NY 10032, USA. M. E. Burns and D. A. Baylor, Department of Neurobiology, Stanford University School of Medicine, Stanford, CA 94305, USA. P. D. Calvert and V. Y. Arshavsky, Howe Laboratory of Ophthalmology, Harvard Medical School, and the Massachusetts Eye and Ear Infirmary, Boston, MA 02114, USA. P. Gouras, Edward S. Harkness Eye Institute, Columbia University, College of Physicians and Surgeons, New York, NY 10032, USA. S. P. Goff, Howard Hughes Medical Institute and Department of Biochemistry and Molecular Biophysics, Columbia University, College of Physicians and Surgeons, New York, NY 10032, USA.
*   These authors contributed equally to this work.

dagger    To whom correspondence should be addressed. E-mail: varshavsky{at}meei.harvard.edu

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Science. ISSN 0036-8075 (print), 1095-9203 (online)