Axis formation during Drosophila oogenesis

Current Opinion in Genetics and Development

Volumn 11, Issue 4, 2001, Pages 374-383

  Riechmann, V ^a   Ephrussi, A ^a  

^a EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

MESSENGER RNA;

ANTERIOR POSTERIOR AXIS; CELL FATE; CELL POLARITY; CYTOSKELETON; EMBRYO DEVELOPMENT; EMBRYO PATTERN FORMATION; EXTRACHROMOSOMAL INHERITANCE; GENE ACTIVITY; GENE LOCATION; MEIOSIS; NONHUMAN; OOCYTE DEVELOPMENT; PRIORITY JOURNAL; REVIEW;

EID: 0035427228     PISSN: 0959437X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-437X(00)00207-0     Document Type: Review

References (73)

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15. An egalitarian-BicaudalD complex is essential for oocyte specification and axis determination in Drosophila
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18. Centrosome migration into the Drosophila oocyte is independent of BicD, egl and the organisation of the microtubule cytoskeleton
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25. Par-1 is required for the maintenance of oocyte fate in Drosophila
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29. Cornichon and the EGF receptor signaling process are necessary for both anterior-posterior and dorsal-ventral pattern formation in Drosophila
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31. Combined activities of Gurken and Decapentaplegic specify dorsal chorion structures of the Drosophila egg
32. Merlin, the Drosophila homologue of Neurofibromatosis-2, is specifically required in posterior follicle cells for axis formation in the oocyte
33. Laminin A is required for follicle cell oocyte signaling that leads to establishment of the anterior-posterior axis in Drosophila
34. Initial organization of the Drosophila dorsoventral axis depends on an RNA-binding protein encoded by the squid gene
35. Specific isoforms of Squid, a Drosophila hnRNP, perform distinct roles in Gurken localization during oogenesis
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43. The Drosophila homolog of C. elegans PAR-1 organizes the oocyte cytoskeleton and directs oskar mRNA localization to the posterior pole
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45. An interaction type of genetic screen reveals a role of the Rab11 gene in oskar mRNA localization in the developing Drosophila melanogaster oocyte
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50. The molecular motor Dynein is involved in targeting Swallow and bicoid RNA to the anterior pole of Drosophila oocytes
51. Mutations that perturb poly(A)-dependent maternal mRNA activation block the initiation of development
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53. Staufen, a gene required to localize maternal RNAs in the Drosophila egg
54. Translational regulation of oskar mRNA by Bruno, an ovarian RNA-binding protein, is essential
55. A function for Kinesin I in the posterior transport of oskar mRNA and Staufen protein
56. Isolation of a ribonucleoprotein complex involved in mRNA localization in Drosophila oocytes
57. Localization-dependent translation requires a functional interaction between the 5′ and 3′ ends of oskar mRNA
58. Translational repressor Bruno plays multiple roles in development and is widely conserved
59. Translational regulation of oskar mRNA occurs independent of the cap and poly(A) tail in Drosophila ovarian extracts
60. Control of oskar mRNA translation by Bruno in a novel cell-free system from Drosophila ovaries
61. The Drosophila CPEB homolog, Orb, is required for Oskar protein expression in oocytes
62. Oskar protein interaction with Vasa represents an essential step in polar granule assembly
63. Translational control of oskar generates short OSK, the isoform that induces pole plasma assembly
64. Localization of oskar RNA regulates oskar translation and requires Oskar protein
65. A conserved 90 nucleotide element mediates translational repression of nanos RNA
66. Vasa mediates translation through interaction with a Drosophila yIF2 homolog
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68. Role for mRNA localization in translational activation but not spatial restriction of nanos RNA
69. Overlapping but distinct RNA elements control repression and activation of nanos translation
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71. Smaug, a novel RNA-binding protein that operates a translational switch in Drosophila
72. Smaug, a novel and conserved protein, contributes to repression of nanos mRNA translation in vitro
73. Synthesis of the posterior determinant Nanos is spatially restricted by a novel cotranslational regulatory mechanism