lethal giant larvae is required with the par genes for the early polarization of the Drosophila oocyte.
Most cell types in an organism show some degree of polarization, which relies on a surprisingly limited number of proteins. The underlying molecular mechanisms depend, however, on the cellular context. Mutual inhibitions between members of the Par genes are proposed to be sufficient to polarize the C. elegans one-cell zygote and the Drosophila oocyte during mid-oogenesis. By contrast, the Par genes interact with cellular junctions and associated complexes to polarize epithelial cells. The Par genes are also required at an early step of Drosophila oogenesis for the maintenance of the oocyte fate and its early polarization. Here we show that the Par genes are not sufficient to polarize the oocyte early and that the activity of the tumor-suppressor gene lethal giant larvae (lgl) is required for the posterior translocation of oocyte-specific proteins, including germline determinants. We also found that Lgl localizes asymmetrically within the oocyte and is excluded from the posterior pole. We further demonstrate that phosphorylation of Par-1, Par-3 (Bazooka) and Lgl is crucial to regulate their activity and localization in vivo and describe, for the first time, adherens junctions located around the ring canals, which link the oocyte to the other cells of the germline cyst. However, null mutations in the DE-cadherin gene, which encodes the main component of the zonula adherens, do not affect the early polarization of the oocyte. We conclude that, despite sharing many similarities with other model systems at the genetic and cellular levels, the polarization of the early oocyte relies on a specific subset of polarity proteins.
Fichelson
Pierre
P
Institut Jacques Monod, CNRS-Universite Paris Diderot, Bât. Buffon -15 rue Hélène Brion, 75205 Paris cedex 13, France.
Jagut
Marlène
M
Lepanse
Sophie
S
Lepesant
Jean-Antoine
JA
Huynh
Jean-René
JR
D000818:Animals; D030801:Animals, Genetically Modified; D016764:Cell Polarity / Q000235:genetics*; D004330:Drosophila / Q000235:genetics* / Q000502:physiology*; D029721:Drosophila Proteins / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D005260:Female; D038362:Glycogen Synthase Kinase 3; D047908:Intracellular Signaling Peptides and Proteins / Q000235:genetics / Q000378:metabolism / Q000502:physiology; D008954:Models, Biological; D009865:Oocytes / Q000378:metabolism / Q000502:physiology*; D009866:Oogenesis / Q000235:genetics / Q000502:physiology; D010053:Ovary / Q000166:cytology / Q000378:metabolism / Q000502:physiology; D010766:Phosphorylation / Q000235:genetics; D017346:Protein Serine-Threonine Kinases / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D013997:Time Factors; D025521:Tumor Suppressor Proteins / Q000235:genetics / Q000378:metabolism / Q000502:physiology*
D029721:Drosophila Proteins; D047908:Intracellular Signaling Peptides and Proteins; D025521:Tumor Suppressor Proteins; C400774:baz protein, Drosophila; C081435:l(2)gl protein, Drosophila; D017346:Protein Serine-Threonine Kinases; D038362:Glycogen Synthase Kinase 3; C472496:Par-1 protein, Drosophila