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Science 27 April 1990:
Vol. 248. no. 4954, pp. 483 - 486
DOI: 10.1126/science.2158671
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Articles
Science, Vol 248, Issue 4954, 483-486
Copyright © 1990 by American Association for the Advancement of Science
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
Department of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City 73190.
The gene encoding the 49-kilodalton protein that undergoes light-induced phosphorylation in the Drosophila photoreceptor has been isolated and characterized. The encoded protein has 401 amino acid residues and a molecular mass of 44,972 daltons, and it shares approximately 42 percent amino acid sequence identity with arrestin (S-antigen), which has been proposed to quench the light-induced cascade of guanosine 3',5'-monophosphate hydrolysis in vertebrate photoreceptors. Unlike the 49-kilodalton protein, however, arrestin, which appears to bind to phosphorylated rhodopsin, has not itself been reported to undergo phosphorylation. In vitro, Ca2+ was the only agent found that would stimulate the phosphorylation of the 49-kilodalton protein. The phosphorylation of this arrestin-like protein in vivo may therefore be triggered by a Ca2+ signal that is likely to be regulated by light-activated phosphoinositide-specific phospholipase C.
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