Abstract
PHOSPHORYLATION of rhodopsin has been studied so far only in vitro. When suspensions of isolated and purified rod outer segments (ROS) from cattle and frogs have been mixed with γ–32P–ATP and Mg2+, upon illumination 32P–phosphate has been found to be bound covalently to rhodopsin in a slow dark reaction after bleaching. The activity of the water-extractable kinase which mediates the phosphate transfer was found to be independent of light, but rhodopsin was not acceptable as a substrate until it had been bleached by light4. The slow rate at which phosphorylation occurs (half time 3–5 min (refs 1–4)) suggests that it may be involved in light adaptation of the rods which also seems to be a slow process5.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References
Kühn, H., and Dreyer, W. J., FEBS Lett., 20, 1–6 (1972).
Bownds, D., Dawes, J., Miller, J., and Stahlman, M., Nature new Biol., 237, 125–127 (1972).
Frank, R. N., Cavanagh, H. D., and Kenyon, K. R., J. biol. Chem., 248, 596–609 (1973).
Kühn, H., Cook, J. H., and Dreyer, W. J., Biochemistry, 12, 2495–2502 (1973).
Dowling, J. E., and Ripps, H., J. gen. Physiol., 60, 698–719 (1972).
Bownds, D., Dawes, J., and Miller, J., in Biochemistry and Physiology of Visual Pigments (edit. by Langer, H.), 267–273 (Springer-Verlag, Berlin, Heidelberg, New York, 1973).
Hall, M. O., and Bacharach, A. D. E., Nature, 225, 637–638 (1970).
McConnell, D. G., J. Cell Biol., 27, 459–473 (1965).
Fairbanks, G., Steck, T. L., and Wallach, D. F. H., Biochemistry, 10, 2606–2617 (1971).
Bownds, D., Gordon-Walker, A., Gaide-Huguenin, A. C., and Robinson, W., J. gen. Physiol., 58, 225–237 (1971).
Bligh, E. G., and Dyer, W. J., Can. J. Biochem. Physiol., 37, 911–917 (1959).
Kohlrausch, A., Handb. Norm. Pathol. Physiol., 12/2, 1499–1594 (Springer-Verlag, Berlin, 1931).
Rushton, W. A. H., J. Physiol., Lond., 156, 193–205 (1961).
Hood, D. C., Hock, P. A., and Grover, B. G., Vision Res., 13, 1953–1963 (1973).
Norman, R. A., and Werblin, F. S., J. gen. Physiol., 63, 37–61 (1974).
Rushton, W. A. H., and Powell, D. S., Vision Res., 12, 1073–1081 (1972).
Grabowski, S. R., Pinto, L. H., and Pak, W. L., Science, 176, 1240–1242 (1972).
Jan, L. Y., and Revel, J. P., J. Cell Biol. (in the press).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
KÜHN, H. Light-dependent phosphorylation of rhodopsin in living frogs. Nature 250, 588–590 (1974). https://doi.org/10.1038/250588a0
Received:
Revised:
Published:
Issue Date:
DOI: https://doi.org/10.1038/250588a0
- Springer Nature Limited
This article is cited by
-
Separation of photoreceptor cell compartments in mouse retina for protein analysis
Molecular Neurodegeneration (2017)
-
Rhodopsin inactivation is a modulated process in Limulus photoreceptors
Nature (1992)
-
Desensitization of the nicotinic acetylcholine receptor: Molecular mechanisms and effect of modulators
Cellular and Molecular Neurobiology (1989)
-
Light-adaptation in the photophobic response by Stentor coeruleus
Archives of Microbiology (1987)
-
Reversible phosphorylation of opsin induced by irradiation of blowfly retinae
Journal of Comparative Physiology A (1984)