Abstract
Bicoid (Bcd) is a morphogenetic protein that instructs patterning along the anterior–posterior (A–P) axis in Drosophila melanogaster embryos. Despite extensive studies, what controls the formation of a normal concentration gradient of Bcd remains an unresolved and controversial question. Here, we show that Bcd protein degradation is mediated by the ubiquitin-proteasome pathway. We have identified an F-box protein, encoded by fates-shifted (fsd), that has an important role in Bcd protein degradation by targeting it for ubiquitylation. Embryos from females lacking fsd have an altered Bcd gradient profile, resulting in a shift of the fatemap along the A–P axis. Our study is an experimental demonstration that, contrary to an alternative hypothesis, Bcd protein degradation is required for normal gradient formation and developmental fate determination.
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Acknowledgements
We thank members of our groups at CCHMC, in particular F. He, D. Cheung, W. Dui, and J. Deng, for discussion and assistance, and we thank Xinhua Lin's lab for some of the primers used in our dsRNAi screening. This work was supported in part by grants from NIH and NSF (to J.M.).
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J.L. and J.M. conceived and designed the study. J.L. performed all experiments and analysis. J.L. and J.M. interpreted the data, J.L. generated all figures and J.L. and J.M. wrote the paper.
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Liu, J., Ma, J. Fates-shifted is an F-box protein that targets Bicoid for degradation and regulates developmental fate determination in Drosophila embryos. Nat Cell Biol 13, 22–29 (2011). https://doi.org/10.1038/ncb2141
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DOI: https://doi.org/10.1038/ncb2141
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