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You are here: Home / Teams / Apoptosis and Neurogenetics - B. Mollereau / Publications / Ferritin Assembly in Enterocytes of Drosophila melanogaster.

Ferritin Assembly in Enterocytes of Drosophila melanogaster.

Abraham Rosas-Arellano, Johana Vasquez-Procopio, Alexis Gambis, Liisa M Blowes, Hermann Steller, Bertrand Mollereau, and Fanis Missirlis (2016)

Int J Mol Sci, 17(2):27.

Ferritins are protein nanocages that accumulate inside their cavity thousands ofoxidized iron atoms bound to oxygen and phosphates. Both characteristic types ofeukaryotic ferritin subunits are present in secreted ferritins from insects, buthere dimers between Ferritin 1 Heavy Chain Homolog (Fer1HCH) and Ferritin 2 Light Chain Homolog (Fer2LCH) are further stabilized by disulfide-bridge in the 24-subunit complex. We addressed ferritin assembly and iron loading in vivo using novel transgenic strains of Drosophila melanogaster. We concentrated on the intestine, where the ferritin induction process can be controlled experimentallyby dietary iron manipulation. We showed that the expression pattern of Fer2LCH-Gal4 lines recapitulated iron-dependent endogenous expression of the ferritin subunits and used these lines to drive expression from UAS-mCherry-Fer2LCH transgenes. We found that the Gal4-mediated induction of mCherry-Fer2LCH subunits was too slow to effectively introduce them into newly formed ferritin complexes. Endogenous Fer2LCH and Fer1HCH assembled and stored excess dietary iron, instead. In contrast, when flies were genetically manipulated to co-express Fer2LCH and mCherry-Fer2LCH simultaneously, both subunits were incorporated with Fer1HCH in iron-loaded ferritin complexes. Our study provides fresh evidence that, in insects, ferritin assembly and iron loading in vivo are tightly regulated.

 
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