Ferritin, a symmetrical 24-subunit heteropolymer composed of heavy and light chains, is the primary iron-storage molecule in bacteria, plants and animals. We used a genetically engineered strain of the model organism Drosophila melanogaster which expresses a GFP (green fluorescent protein)-tagged ferritin 1 heavy chain homologue from its native chromosomal locus and incorporated it into endogenous functional ferritin, enabling in vivo visualization of the protein and permitting easy assessment of ferritin status following environmental or genetic perturbations. Random mutagenesis was induced, and individual mutagenized chromosomes were recovered by classic crossing schemes involving phenotypical markers and balancer chromosomes. In wild-type larvae, ferritin is predominantly localized in the brain, in regions of the intestine, in wreath cells and in pericardial cells. A pilot genetic screen revealed a mutant fruitfly strain expressing GFP–ferritin in the anal pads, a pair of organs located ventrally in the posterior end of the fruitfly larva, possibly involved in ion absorption and osmoregulation, which are normally devoid of ferritin. Our continuing genetic screen could reveal transcription factors involved in ferritin regulation and novel proteins important in iron metabolism, hopefully with conserved functions in evolution.