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Science 13 January 1984:
Vol. 223. no. 4632, pp. 184 - 186
DOI: 10.1126/science.6419348
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Articles

Science, Vol 223, Issue 4632, 184-186
Copyright © 1984 by American Association for the Advancement of Science

articles

Light-induced phosphorylation of retina-specific polypeptides of Drosophila in vivo

H Matsumoto and WL Pak

A moderate light stimulus induced isoelectric point (pI) changes in three classes of retina-specific polypeptides (80, 49, and 39 kilodaltons) of Drosophila in vivo. When inorganic phosphate labeled with phosphorus-32 was fed to flies, the radioactive label was incorporated into these polypeptides during the pI changes, indicating light-induced phosphorylation of the polypeptides. A 1-millisecond flash induced a detectable amount of phosphorylation in the 80- and 49-kilodalton polypeptides within 3 seconds. These results, and our previous results with norpA mutants, suggest that phosphorylation of these two polypeptides may be involved in some early stages of photoreceptor excitation or its modulation.


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Mechanism of Phosphorylation-Recognition by Visual Arrestin and the Transition of Arrestin into a High Affinity Binding State.
V. V. Gurevich and J. L. Benovic (1997)
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Phosphorylation of the InaD Gene Product, a Photoreceptor Membrane Protein Required for Recovery of Visual Excitation.
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A 49-kilodalton phosphoprotein in the Drosophila photoreceptor is an arrestin homolog.
T Yamada, Y Takeuchi, N Komori, H Kobayashi, Y Sakai, Y Hotta, and H Matsumoto (1990)
Science 248, 483-486
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Neuronal phosphoproteins: physiological and clinical implications.
E. Nestler, S. Walaas, and P Greengard (1984)
Science 225, 1357-1364
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