lethal giant larvae is required with the par genes for the early polarization of the Drosophila oocyte.
ABSTRACT 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.
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ABSTRACT: Within the short span of the cell cycle, poly(ADP-ribose) (pADPr) can be rapidly produced by poly(ADP-ribose) polymerases and degraded by poly(ADP-ribose) glycohydrolases. Here we show that changes in association between pADPr and heterogeneous nuclear ribonucleoproteins (hnRNPs) regulate germline stem cell (GSC) maintenance and egg chamber polarity during oogenesis in Drosophila. The association of pADPr and Hrp38, an orthologue of human hnRNPA1, disrupts the interaction of Hrp38 with the 5'-untranslated region of DE-cadherin messenger RNA, thereby diminishing DE-cadherin translation in progenitor cells. Following the reduction of DE-cadherin level, GSCs leave the stem cell niche and differentiate. Defects in either pADPr catabolism or Hrp38 function cause a decrease in DE-cadherin translation, leading to a loss of GSCs and mislocalization of oocytes in the ovary. Taken together, our findings suggest that Hrp38 and its association with pADPr control GSC self-renewal and oocyte localization by regulating DE-cadherin translation.Nature Communications 01/2012; 3:760. · 10.02 Impact Factor
- 02/2012; , ISBN: 978-953-307-879-3
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ABSTRACT: The Drosophila dorsal-ventral (DV) axis is polarized when the oocyte nucleus migrates from the posterior to the anterior margin of the oocyte. Prior work suggested that dynein pulls the nucleus to the anterior side along a polarized microtubule cytoskeleton, but this mechanism has not been tested. By imaging live oocytes, we find that the nucleus migrates with a posterior indentation that correlates with its direction of movement. Furthermore, both nuclear movement and the indentation depend on microtubule polymerization from centrosomes behind the nucleus. Thus, the nucleus is not pulled to the anterior but is pushed by the force exerted by growing microtubules. Nuclear migration and DV axis formation therefore depend on centrosome positioning early in oogenesis and are independent of anterior-posterior axis formation.Science 04/2012; 336(6084):999-1003. · 31.20 Impact Factor