Fates-shifted is an F-box protein that targets Bicoid for degradation and regulates developmental fate determination in Drosophila embryos

Nature Cell Biology

Volumn 13, Issue 1, 2011, Pages 22-29

  Liu, Junbo ^a   Ma, Jun ^a  

^a CINCINNATI CHILDREN S HOSPITAL RESEARCH FOUNDATION   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BICOID; F BOX PROTEIN; MEMBRANE PROTEIN; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; DROSOPHILA MELANOGASTER; EMBRYO; IMMUNOPRECIPITATION; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROMOTER REGION; PROTEIN ANALYSIS; PROTEIN DEGRADATION; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; RNA INTERFERENCE; SEQUENCE ANALYSIS; UBIQUITINATION;

AMINO ACID SEQUENCE; ANIMALS; BLOTTING, WESTERN; BODY PATTERNING; CELL LINE; CYSTEINE PROTEINASE INHIBITORS; DROSOPHILA MELANOGASTER; DROSOPHILA PROTEINS; 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; PROTEIN BINDING; RNA INTERFERENCE; SEQUENCE HOMOLOGY, AMINO ACID; TRANS-ACTIVATORS; UBIQUITIN;

DROSOPHILA MELANOGASTER;

EID: 78650511745     PISSN: 14657392     EISSN: None     Source Type: Journal    
DOI: 10.1038/ncb2141     Document Type: Article

References (64)

1. Wolpert, L. Positional information and the spatial pattern of cellular differentiation. J. Theor. Biol 25, 1-47 (1969).
2. Kerszberg, M. & Wolpert, L. Specifying positional information in the embryo: looking beyond morphogens. Cell 130, 205-209 (2007).
3. Lander, A. D. Morpheus unbound: reimagining the morphogen gradient. Cell 128, 245-256 (2007).
4. Martinez Arias, A. & Hayward, P. Filtering transcriptional noise during development: concepts and mechanisms. Nat. Rev. Genet. 7, 34-44 (2006).
5. Wartlick, O., Kicheva, A. & Gonzalez Gaitan, M. Morphogen gradient formation. Cold Spring Harb. Perspect. Biol. 1, a001255 (2009).
6. Ephrussi, A. & St. Johnston, D. Seeing is believing. The bicoid morphogen gradient matures. Cell 116, 143-152 (2004).
7. Driever, W. & Nüsslein Volhard, C. A gradient of bicoid protein in Drosophila embryos. Cell 54, 83-93 (1988).
8. Struhl, G., Struhl, K. & Macdonald, P. The gradient morphogen bicoid is a concen tration dependent transcriptional activator. Cell 57, 1259-1273 (1989).
9. Driever, W., Thoma, G. & Nüsslein Volhard, C. Determination of spatial domains of zygotic gene expression in the Drosophila embryo by the affinity of binding site for the bicoid morphogen. Nature 340, 363-367 (1989).
10. Deng, J., Wang, W., Lu, L. J. & Ma, J. A two dimensional simulation model of the Bicoid gradient in Drosophila. PLoS ONE 5, e10275 (2010).
11. Bergmann, S. et al. Presteady state decoding of the Bicoid morphogen gradient. PLoS biology 5, e46 (2007).
12. Gregor, T., Bialek, W., van Steveninck, R. R., Tank, D. W. & Wieschaus, E. F. Diffusion and scaling during early embryonic pattern formation. Proc. Natl Acad. Sci. USA 102, 18403-18407 (2005).
13. Gregor, T., Wieschaus, E. F., McGregor, A. P., Bialek, W. & Tank, D. W. Stability and nuclear dynamics of the bicoid morphogen gradient. Cell 130, 141-152 (2007).
14. Porcher, A. et al. The time to measure positional information: maternal hunchback is required for the synchrony of the Bicoid transcriptional response at the onset of zygotic transcription. Development 137, 2795-2804 (2010).
15. Zhao, C. et al. The activity of the Drosophila morphogenetic protein Bicoid is inhibited by a domain located outside its homeodomain. Development 129, 1669-1680 (2002).
16. Fenteany, G. et al. Inhibition of proteasome activities and subunit specific amino terminal threonine modification by lactacystin. Science 268, 726-731 (1995).
17. Meng, L. et al. Epoxomicin, a potent and selective proteasome inhibitor, exhibits in vivo antiinflammatory activity. Proc. Natl Acad. Sci. USA 96, 10403-10408 (1999).
18. Belle, A., Tanay, A., Bitincka, L., Shamir, R. & O'Shea, E. K. Quantification of protein half lives in the budding yeast proteome. Proc. Natl Acad. Sci. USA 103, 13004-13009 (2006).
19. Pickart, C. M. Mechanisms underlying ubiquitination. Annu. Rev. Biochem. 70, 503-533 (2001).
20. Pickart, C. M. & Eddins, M. J. Ubiquitin: structures, functions, mechanisms. Biochim. Biophys. Acta 1695, 55-72 (2004).
21. Herrmann, J., Lerman, L. O. & Lerman, A. Ubiquitin and ubiquitin like proteins in protein regulation. Circ. Res. 100, 1276-1291 (2007).
22. Ciechanover, A. Proteolysis: from the lysosome to ubiquitin and the proteasome. Nat. Rev. Mol. Cell Biol. 6, 79-87 (2005).
23. Hershko, A., Ganoth, D., Pehrson, J., Palazzo, R. E. & Cohen, L. H. Methylated ubiquitin inhibits cyclin degradation in clam embryo extracts. J. Biol. Chem. 266, 16376-16379 (1991).
24. Hsu, T., McRackan, D., Vincent, T. S. & Gert de Couet, H. Drosophila Pin1 prolyl isomerase Dodo is a MAP kinase signal responder during oogenesis. Nat. Cell Biol. 3, 538-543 (2001)
25. Deshaies, R. J. SCF and Cullin/Ring H2 based ubiquitin ligases. Annu. Rev. Cell Dev. Biol. 15, 435-467 (1999).
26. Conaway, R. C., Brower, C. S. & Conaway, J. W. Emerging roles of ubiquitin in tran scription regulation. Science 296, 1254-1258 (2002).
27. Muratani, M., Kung, C., Shokat, K. M. & Tansey, W. P. The F box protein Dsg1/Mdm30 is a transcriptional coactivator that stimulates Gal4 turnover and cotranscriptional mRNA processing. Cell 120, 887-899 (2005).
28. Von der Lehr, N. et al. The F box protein Skp2 participates in cMyc proteosomal degradation and acts as a cofactor for c Myc regulated transcription. Mol. Cell 11, 1189-1200 (2003).
29. Kornitzer, D., Raboy, B., Kulka, R. G. & Fink, G. R. Regulated degradation of the transcription factor Gcn4. EMBO J. 13, 6021-6030 (1994).
30. Jiang, J. & Struhl, G. Regulation of the Hedgehog and Wingless signalling pathways by the F box/WD40 repeat protein Slimb. Nature 391, 493-496 (1998).
31. Kipreos, E. T. & Pagano, M. The F box protein family. Genome Biol 1, reviews3002-reviews3002.7 (2000).
32. Ho, M. S., Tsai, P. I. & Chien, C. T. F box proteins: the key to protein degradation. J. Biomed. Sci. 13, 181-191 (2006).
33. Frohnhöfer, H. G. & Nüsslein Volhard, C. Organization of anterior pattern in the Drosophila embryo by the maternal gene bicoid. Nature 324, 120-125 (1986).
34. Berleth, T. et al. The role of localization of bicoid RNA in organizing the anterior pat tern of the Drosophila embryo. EMBO J. 7, 1749-1756 (1988).
35. Driever, W., Siegel, V. & Nüsslein Volhard, C. Autonomous determination of anterior structures in the early Drosophila embryo by the bicoid morphogen. Development 109, 811-820 (1990).
36. Driever, W. & Nüsslein Volhard, C. The bicoid protein determines position in the Drosophila embryo in a concentration dependent manner. Cell 54, 95-104 (1988).
37. Small, S., Kraut, R., Hoey, T., Warrior, R. & Levine, M. Transcriptional regulation of a pair rule stripe in Drosophila. Genes & Dev. 5, 827-839 (1991).
38. RiverA-Pomar, R. & Jackle, H. From gradients to stripes in Drosophila embryogenesis: filling in the gaps. Trends Genet. 12, 478-483 (1996).
39. Driever, W. & Nüsslein Volhard, C. Bicoid protein is a positive regulator of hunchback transcription in the early Drosophila embryo. Nature 337, 138-143 (1989).
40. Perkins, T. J., Jaeger, J., Reinitz, J. & Glass, L. Reverse engineering the gap gene network of Drosophila melanogaster. PLoS Comput. Biol. 2, e51 (2006).
41. Schaeffer, V., Janody, F., Loss, C., Desplan, C. & Wimmer, E. A. Bicoid functions without its TATA binding protein associated factor interaction domains. Proc. Natl Acad. Sci. USA 96, 4461-4466 (1999).
42. Houchmandzadeh, B., Wieschaus, E. & Leibler, S. Establishment of developmental precision and proportions in the early Drosophila embryo. Nature 415, 798-802 (2002).
43. Crauk, O. & Dostatni, N. Bicoid determines sharp and precise target gene expression in the Drosophila embryo. Curr. Biol. 15, 1888-1898 (2005).
44. Rivera Pomar, R., Lu, X., Taubert, H., Perrimon, N. & Jackle, H. Activation of posterior gap gene expression in the Drosophila blastoderm. Nature 376, 253-256 (1995).
45. He, F. et al. Probing intrinsic properties of a robust morphogen gradient in Drosophila. Dev. Cell 15, 558-567 (2008).
46. He, F. et al. Shaping a morphogen gradient for positional precision. Biophys. J. 99, 697-707 (2010).
47. Coppey, M., Berezhkovskii, A. M., Kim, Y., Boettiger, A. N. & Shvartsman, S. Y. Modeling the bicoid gradient: diffusion and reversible nuclear trapping of a stable protein. Dev. Biol. 312, 623-630 (2007).
48. Spirov, A. et al. Formation of the bicoid morphogen gradient: an mRNA gradient dictates the protein gradient. Development 136, 605-614 (2009).
49. He, F. et al. Distance measurements via the morphogen gradient of Bicoid in Drosophila embryos. BMC Dev. Biol. 10, 80 (2010).
50. Jaeger, J. et al. Dynamic control of positional information in the early Drosophila embryo. Nature 430, 368-371 (2004).
51. Manu et al. Canalization of gene expression in the Drosophila blastoderm by gap gene cross regulation. PLoS biology 7, e1000049 (2009).
52. Lucchetta, E. M., Vincent, M. E. & Ismagilov, R. F. A precise Bicoid gradient is nonessential during cycles 11-13 for precise patterning in the Drosophila blas toderm. PLoS One 3, e3651 (2008).
53. Hecht, I., Rappel, W. J. & Levine, H. Determining the scale of the Bicoid morphogen gradient. Proc. Natl Acad. Sci. USA 106, 1710-1715 (2009).
54. Gregor, T., McGregor, A. P. & Wieschaus, E. F. Shape and function of the Bicoid morphogen gradient in dipteran species with different sized embryos. Dev. Biol. 316, 350-358 (2008).
55. Grimm, O. & Wieschaus, E. The Bicoid gradient is shaped independently of nuclei. Development 137, 2857-2862 (2010).
56. Fu, D. & Ma, J. Interplay between positive and negative activities that influence the role of Bicoid in transcription. Nucleic acids research 33, 3985-3993 (2005).
57. Fu, D., Wen, Y. & Ma, J. The coactivator CREB binding protein participates in enhancer dependent activities of Bicoid. J. Biol. Chem. 279, 48725-48733 (2004).
58. Forler, D. et al. An efficient protein complex purification method for functional proteomics in higher eukaryotes. Nat. Biotechnol. 21, 89-92 (2003).
59. Crevel, G. & Cotterill, S. DNA replication in cell free extracts from Drosophila mela-nogaster. EMBO J. 10, 4361-4369 (1991).
60. Clemens, J. C. et al. Use of double stranded RNA interference in Drosophila cell lines to dissect signal transduction pathways. Proc. Natl Acad. Sci. USA 97, 6499-6503 (2000).
61. Tautz, D. & Pfeifle, C. A non radioactive in situ hybridization method for the localization of specific RNAs in Drosophila embryos reveals translational control of the segmentation gene hunchback. Chromosoma 98, 81-85 (1989).
62. Kosman, D. et al. Multiplex detection of RNA expression in Drosophila embryos. Science 305, 846 (2004).
63. Surkova, S. et al. Characterization of the Drosophila segment determination morphome. Developmental biology 313, 844-862 (2008).
64. Lattin, J., Carroll, J. D. & Green, P. E. Analyzing multivariate data. (Thompson Books/ Cole, 2003).