Fates-shifted is an F-box protein that targets Bicoid for degradation and regulates developmental fate determination in Drosophila embryos.
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.
Pubmed ID: 21170036 RIS Download
Amino Acid Sequence | Animals | Blotting, Western | Body Patterning | Cell Line | Cysteine Proteinase Inhibitors | Drosophila Proteins | Drosophila melanogaster | Embryo, Nonmammalian | F-Box Proteins | Female | Gene Expression Regulation, Developmental | HEK293 Cells | Homeodomain Proteins | Humans | Immunoprecipitation | In Situ Hybridization | Leupeptins | Male | Molecular Sequence Data | Proteasome Endopeptidase Complex | Proteasome Inhibitors | Protein Binding | RNA Interference | Sequence Homology, Amino Acid | Trans-Activators | Ubiquitin