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

被引:169
作者
Tsang, SH
Burns, ME
Calvert, PD
Gouras, P
Baylor, DA
Goff, SP
Arshavsky, VY [1 ]
机构
[1] Harvard Univ, Sch Med, Howe Lab Ophthalmol, Boston, MA 02114 USA
[2] Columbia Univ Coll Phys & Surg, Edward S Harkness Eye Inst, New York, NY 10032 USA
[3] Columbia Univ Coll Phys & Surg, Dept Biochem & Mol Biophys, New York, NY 10032 USA
[4] Stanford Univ, Sch Med, Dept Neurobiol, Stanford, CA 94305 USA
[5] Massachusetts Eye & Ear Infirm, Boston, MA 02114 USA
[6] Columbia Univ Coll Phys & Surg, Howard Hughes Med Inst, New York, NY 10032 USA
关键词
D O I
10.1126/science.282.5386.117
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Heterotrimeric guanosine 5'-triphosphate (GTP)-binding proteins (C proteins) are deactivated by hydrolysis of the CTP that they bind when activated by transmembrane receptors. Transducin, the C 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.
引用
收藏
页码:117 / 121
页数:5
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