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      Drosophila phosphopantothenoylcysteine synthetase is required for tissue morphogenesis during oogenesis

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          Abstract

          Background

          Coenzyme A (CoA) is an essential metabolite, synthesized from vitamin B 5 by the subsequent action of five enzymes: PANK, PPCS, PPCDC, PPAT and DPCK. Mutations in Drosophila dPPCS disrupt female fecundity and in this study we analyzed the female sterile phenotype of dPPCS mutants in detail.

          Results

          We demonstrate that dPPCS is required for various processes that occur during oogenesis including chorion patterning. Our analysis demonstrates that a mutation in dPPCS disrupts the organization of the somatic and germ line cells, affects F-actin organization and results in abnormal PtdIns(4,5)P 2 localization. Improper cell organization coincides with aberrant localization of the membrane molecules Gurken (Grk) and Notch, whose activities are required for specification of the follicle cells that pattern the eggshell. Mutations in dPPCS also induce alterations in scutellar patterning and cause wing vein abnormalities. Interestingly, mutations in dPANK and dPPAT-DPCK result in similar patterning defects.

          Conclusion

          Together, our results demonstrate that de novo CoA biosynthesis is required for proper tissue morphogenesis.

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          Most cited references 21

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          Stem cells and their progeny respond to nutritional changes during Drosophila oogenesis.

          Understanding how stem-cell proliferation is controlled to maintain adult tissues is of fundamental importance. Drosophila oogenesis provides an attractive system to study this issue since cell production in the ovary depends on small populations of observable germ-line and somatic stem cells. By controlling the amount of protein-rich nutrients in the diet, we established conditions under which the rate of egg production varied 60-fold. Using a cell-lineage labeling system, we found that both germ-line and somatic stem cells, as well as their progeny, adjust their proliferation rates in response to nutrition. However, the number of active stem cells does not appear to change. Proliferation rates varied fourfold; the remaining 15-fold difference in egg production resulted from different frequencies of cell death at two precise developmental points: (1) the region 2a/2b transition within the germarium, and (2) stage 8 egg chambers that are entering vitellogenesis. To initiate a genetic analysis of these changes in cell proliferation and apoptosis, we show that ovarian cells require an intact insulin pathway to fully upregulate their rate of cycling in response to a protein-rich diet and to enter vitellogenesis.
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            Mass transit: epithelial morphogenesis in the Drosophila egg chamber.

            Epithelial cells use a striking array of morphogenetic behaviors to sculpt organs and body plans during development. Although it is clear that epithelial morphogenesis is largely driven by cytoskeletal rearrangements and changes in cell adhesion, little is known about how these processes are coordinated to construct complex biological structures from simple sheets of cells. The follicle cell epithelium of the Drosophila egg chamber exhibits a diverse range of epithelial movements in a genetically accessible tissue, making it an outstanding system for the study of epithelial morphogenesis. In this review, we move chronologically through the process of oogenesis, highlighting the dynamic movements of the follicle cells. We discuss the cellular architecture and patterning events that set the stage for morphogenesis, detail individual cellular movements, and focus on current knowledge of the cellular processes that drive follicle cell behavior. Copyright (c) 2005 Wiley-Liss, Inc.
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              Direct association of Bazooka/PAR-3 with the lipid phosphatase PTEN reveals a link between the PAR/aPKC complex and phosphoinositide signaling.

              Cell polarity in Drosophila epithelia, oocytes and neuroblasts is controlled by the evolutionarily conserved PAR/aPKC complex, which consists of the serine-threonine protein kinase aPKC and the PDZ-domain proteins Bazooka (Baz) and PAR-6. The PAR/aPKC complex is required for the separation of apical and basolateral plasma membrane domains, for the asymmetric localization of cell fate determinants and for the proper orientation of the mitotic spindle. How the complex exerts these different functions is not known. We show that the lipid phosphatase PTEN directly binds to Baz in vitro and in vivo, and colocalizes with Baz in the apical cortex of epithelia and neuroblasts. PTEN is an important regulator of phosphoinositide turnover that antagonizes the activity of PI3-kinase. We show that Pten mutant ovaries and embryos lacking maternal and zygotic Pten function display phenotypes consistent with a function for PTEN in the organization of the actin cytoskeleton. In freshly laid eggs, the germ plasm determinants oskar mRNA and Vasa are not localized properly to the posterior cytocortex and pole cells do not form. In addition, the actin-dependent posterior movement of nuclei during early cleavage divisions does not occur and the synchrony of nuclear divisions at syncytial blastoderm stages is lost. Pten mutant embryos also show severe defects during cellularization. Our data provide evidence for a link between the PAR/aPKC complex, the actin cytoskeleton and PI3-kinase signaling mediated by PTEN.
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                Author and article information

                Journal
                BMC Res Notes
                BMC Research Notes
                BioMed Central
                1756-0500
                2008
                29 August 2008
                : 1
                : 75
                Affiliations
                [1 ]Department of Cell Biology, Section of Radiation & Stress Cell Biology, University Medical Center Groningen, University of Groningen, Groningen, The Netherlands
                Article
                1756-0500-1-75
                10.1186/1756-0500-1-75
                2542404
                18759961
                Copyright © 2008 Sibon et al; licensee BioMed Central Ltd.

                This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

                Categories
                Short Report

                Medicine

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