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

Science

Volumn 282, Issue 5386, 1998, Pages 117-121

  Tsang, Stephen H ^a   Burns, Marie E ^b   Calvert, Peter D ^c   Gouras, Peter ^a   Baylor, Denis A ^b   Goff, Stephen P ^d   Arshavsky, Vadim Y ^c  

^a New York Presbyterian Hospital   (United States)

^b STANFORD UNIVERSITY SCHOOL OF MEDICINE   (United States)

^c MASSACHUSETTS EYE AND EAR INFIRMARY   (United States)

^d The New York Presbyterian Hospital   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

GUANINE NUCLEOTIDE BINDING PROTEIN; RHODOPSIN; TRANSDUCIN;

ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL TISSUE; ARTICLE; BINDING AFFINITY; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME ANALYSIS; HYDROLYSIS; MOUSE; NONHUMAN; PHOTORECEPTOR; PRIORITY JOURNAL; PROTEIN INTERACTION; SIGNAL TRANSDUCTION; VISION;

3',5'-CYCLIC-GMP PHOSPHODIESTERASE; ANIMALS; ELECTRORETINOGRAPHY; ENZYME ACTIVATION; FEMALE; GUANOSINE 5'-O-(3-THIOTRIPHOSPHATE); GUANOSINE TRIPHOSPHATE; HYDROLYSIS; LIGHT; MALE; MICE; MICE, KNOCKOUT; MICE, TRANSGENIC; PHOTOTRANSDUCTION; POINT MUTATION; RETINA; RETINAL DEGENERATION; ROD OUTER SEGMENTS; TRANSDUCIN; TRANSGENES;

EID: 0032475826     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.282.5386.117     Document Type: Article

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51. We thank E. R. Makino and J. W. Handy for help with biochemical experiments; D. B. Farber for providing Pdeg cDNA; J. Xu and M. I. Simon for providing the opsin promoters; T. G. Wensel for providing antibodies against RGS9; F. Costantini, C. Liu, and members of their laboratories for sharing ideas and equipment; V. I. Govardovskii, R. Axel, and E. Kandel for critically reading the manuscript; and M. Mendelsohn, K. Doi, H. Kjeldbye, J. Ma, and D. Wiener for discussion. Supported by NIH grants T32 EY07105, EY05750, EY10336, and EY11510; the Ruth and Milton Steinbach Fund; the McKnight Foundation; and Research to Prevent Blindness (RPB). S.P.G. is an investigator of the Howard Hughes Medical Institute. V.Y.A. is a recipient of a Jules and Doris Stein professorship from RPB.