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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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A 49-kilodalton phosphoprotein in the Drosophila photoreceptor is an arrestin homolog.

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.[1]

References

  1. A 49-kilodalton phosphoprotein in the Drosophila photoreceptor is an arrestin homolog. Yamada, T., Takeuchi, Y., Komori, N., Kobayashi, H., Sakai, Y., Hotta, Y., Matsumoto, H. Science (1990) [Pubmed]
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