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Gene Review

BicD  -  Bicaudal D

Drosophila melanogaster

Synonyms: BIC-D, BICD, Bic-D, Bic[D], CG6605, ...
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High impact information on BicD


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].


  1. Requirement for phosphorylation and localization of the Bicaudal-D protein in Drosophila oocyte differentiation. Suter, B., Steward, R. Cell (1991) [Pubmed]
  2. Structure of the Drosophila BicaudalD protein and its role in localizing the the posterior determinant nanos. Wharton, R.P., Struhl, G. Cell (1989) [Pubmed]
  3. An Egalitarian-BicaudalD complex is essential for oocyte specification and axis determination in Drosophila. Mach, J.M., Lehmann, R. Genes Dev. (1997) [Pubmed]
  4. Homeless is required for RNA localization in Drosophila oogenesis and encodes a new member of the DE-H family of RNA-dependent ATPases. Gillespie, D.E., Berg, C.A. Genes Dev. (1995) [Pubmed]
  5. BicD-dependent localization processes: from Drosophilia development to human cell biology. Claussen, M., Suter, B. Ann. Anat. (2005) [Pubmed]
  6. Interaction between Polo and BicD proteins links oocyte determination and meiosis control in Drosophila. Mirouse, V., Formstecher, E., Couderc, J.L. Development (2006) [Pubmed]
  7. A human homologue (BICD1) of the Drosophila bicaudal-D gene. Baens, M., Marynen, P. Genomics (1997) [Pubmed]
  8. Interactions between coiled-coil proteins: Drosophila lamin Dm0 binds to the bicaudal-D protein. Stuurman, N., Häner, M., Sasse, B., Hübner, W., Suter, B., Aebi, U. Eur. J. Cell Biol. (1999) [Pubmed]
  9. The fusome and microtubules enrich Par-1 in the oocyte, where it effects polarization in conjunction with Par-3, BicD, Egl, and dynein. Vaccari, T., Ephrussi, A. Curr. Biol. (2002) [Pubmed]
  10. Embryonic origin of hemocytes and their relationship to cell death in Drosophila. Tepass, U., Fessler, L.I., Aziz, A., Hartenstein, V. Development (1994) [Pubmed]
  11. Spatial and developmental changes in the respiratory activity of mitochondria in early Drosophila embryos. Akiyama, T., Okada, M. Development (1992) [Pubmed]
  12. The role of BicD, Egl, Orb and the microtubules in the restriction of meiosis to the Drosophila oocyte. Huynh, J.R., St Johnston, D. Development (2000) [Pubmed]
  13. Egalitarian binds dynein light chain to establish oocyte polarity and maintain oocyte fate. Navarro, C., Puthalakath, H., Adams, J.M., Strasser, A., Lehmann, R. Nat. Cell Biol. (2004) [Pubmed]
  14. Dominant maternal-effect mutations of Drosophila melanogaster causing the production of double-abdomen embryos. Mohler, J., Wieschaus, E.F. Genetics (1986) [Pubmed]
  15. The Ste20-like kinase misshapen functions together with Bicaudal-D and dynein in driving nuclear migration in the developing drosophila eye. Houalla, T., Hien Vuong, D., Ruan, W., Suter, B., Rao, Y. Mech. Dev. (2005) [Pubmed]
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