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Science 28 August 1992:
Vol. 257. no. 5074, pp. 1255 - 1258
DOI: 10.1126/science.1519062
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Articles

Science, Vol 257, Issue 5074, 1255-1258
Copyright © 1992 by American Association for the Advancement of Science

articles

Deactivation of visual transduction without guanosine triphosphate hydrolysis by G protein

MA Erickson, P Robinson, and J Lisman

Department of Biochemistry, Brandeis University, Waltham, MA 02254.

G proteins couple receptors to their target enzymes in many signal transduction cascades. It has generally been thought that deactivation of such cascades cannot occur without the hydrolysis of guanosine triphosphate (GTP) by G protein. This requirement has now been reexamined in both vertebrate and invertebrate phototransduction. Results indicate that GTP hydrolysis is not required for deactivation. Evidence is presented for an alternative model in which the target enzyme is deactivated by an inhibitory factor that is available even when GTP hydrolysis is blocked.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
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Acceleration of Key Reactions as a Strategy to Elucidate the Rate-Limiting Chemistry Underlying Phototransduction Inactivation.
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Adaptation in Vertebrate Photoreceptors.
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Ca2+/calmodulin-binding peptides block phototransduction in Limulus ventral photoreceptors: Evidence for direct inhibition of phospholipase C.
E. A. Richard, S. Ghosh, J. M. Lowenstein, and J. E. Lisman (1997)
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Regulation of Transducin GTPase Activity by Human Retinal RGS.
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The core domain of a new retina specific RGS protein stimulates the GTPase activity of transducin in vitro.
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Phosphorylation by Cyclin-dependent Protein Kinase 5 of the Regulatory Subunit of Retinal cGMP Phosphodiesterase. II. ITS ROLE IN THE TURNOFF OF PHOSPHODIESTERASE IN VIVO.
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J. Biol. Chem. 275, 32958-32965
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