High impact information on BicD

• Requirement for phosphorylation and localization of the Bicaudal-D protein in Drosophila oocyte differentiation [1].
• Taken together, these results suggest that BicD encodes a cytoskeleton-like protein involved in transporting or anchoring the nanos morphogen within the oocyte cytoplasm [2].
• We have isolated the egl gene and show that Egl protein colocalizes with BicD protein at all stages of oogenesis [3].
• We propose that the Egl-BicD protein complex links microtubule polarity and RNA transport [3].
• In contrast, hu-li tai shao and Bicaudal-D transcripts were transported and localized normally in hls mutants [4].

Biological context of BicD

• In Drosophila, the microtubule-dependent BicD (BicaudalD) localization machinery is involved in the proper localization of mRNA during oogenesis and embryogenesis and the proper positioning of the oocyte and photoreceptor nuclei [5].
• However, the exact mechanism of how BicD-dependent polarized transport could influence meiosis and vice versa remains an open question [6].
• In this article, we report that the cell cycle regulatory kinase Polo binds to BicD protein during oogenesis [6].
• We previously isolated a cDNA fragment homologous to the Drosophila Bicaudal-D gene (Bic-D) using a hybridization selection procedure with cosmids derived from the short arm of human chromosome 12 [7].
• The affinity for lamin Dm0 of the minimal binding site on BICD is modulated in a complex fashion by other BICD segments [8].

Anatomical context of BicD

• At the time of polarization, the kinase itself and the determinant BicaudalD (BicD) are relocalized from the anterior to the posterior of the oocyte [9].
• The Drosophila Bicaudal-D gene encodes a coiled coil protein, characterized by five alpha-helix domains and a leucine zipper motif, that forms part of the cytoskeleton and mediates the correct sorting of mRNAs for oocyte- and axis-determining factors during oogenesis [7].
• Finally, we show that, in the Drosophila embryo, apoptosis can occur independently of macrophages, since mutations lacking macrophages (Bicaudal D; twist snail double mutants; torso4021) show abundant cell death [10].
• The origin of hemocytes from the head mesoderm is further supported by the finding that in Bicaudal D, a mutation that lacks all head structures, and in twist snail double mutants, where no mesoderm develops, hemocytes do not form [10].

Associations of BicD with chemical compounds

• In addition, we found that the anterior of Bicaudal-D mutant embryos at cleavage stage was stained with rhodamine 123 with the same intensity as the posterior of wild-type embryos [11].

Physical interactions of BicD

• Furthermore, unlike all cytoplasmic markers for the oocyte, the SC still becomes restricted to one cell when the microtubules are depolymerised, even though the BicD/Egl complex is not localised [12].
• Interactions between coiled-coil proteins: Drosophila lamin Dm0 binds to the bicaudal-D protein [8].

Other interactions of BicD

• Hence, Egl and BicD, which have been shown to associate, may be part of a conserved core localization machinery in Drosophila, although a direct association between these molecules and the dynein motor complex has not been shown [13].
• This localization is dependent on BicD and the Dynein complex [6].
• Dominant mutations at two loci, BicaudalC (BicC) and BicaudalD (BicD), cause heterozygous females to produce double-abdomen embryos [14].
• The Ste20-like kinase misshapen functions together with Bicaudal-D and dynein in driving nuclear migration in the developing drosophila eye [15].
• In a yeast two-hybrid screen we identified an interaction between Drosophila lamin Dm0, a structural nuclear protein, and BICD, a protein involved in oocyte development [8].

References