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Drosophila phosphopantothenoylcysteine synthetase is required for tissue morphogenesis during oogenesis.


ABSTRACT:

Background

Coenzyme A (CoA) is an essential metabolite, synthesized from vitamin B5 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)P2 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.

SUBMITTER: Bosveld F 

PROVIDER: S-EPMC2542404 | biostudies-literature | 2008 Aug

REPOSITORIES: biostudies-literature

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Drosophila phosphopantothenoylcysteine synthetase is required for tissue morphogenesis during oogenesis.

Bosveld Floris F   Rana Anil A   Lemstra Willy W   Kampinga Harm H HH   Sibon Ody C M OC  

BMC research notes 20080829


<h4>Background</h4>Coenzyme A (CoA) is an essential metabolite, synthesized from vitamin B5 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.<h4>Results</h4>We demonstrate that dPPCS is required for various processes that occur during oogenesis including chorion patterning. Our analysis demonstrates that a mutation in dPPCS disrup  ...[more]

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