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doi:10.1534/genetics.107.075150
A more recent version of this article appeared on September 1, 2007.
REGULAR RESEARCH PAPERS |
Homeostatic Mechanisms for Iron Storage Revealed by Genetic Manipulations and Live Imaging of Drosophila Ferritin
Fanis Missirlis 1*, Stylianos Kosmidis 2, Tom Brody 3, Manos Mavrakis 1, Sara Holmberg 1, Ward F Odenwald 3, Efthimios M. C. Skoulakis 2 and Tracey A Rouault 1
1 National Institute of Child Health and Human Development
2 BSRC
3 NINDS
* To whom correspondence should be addressed. E-mail: missirlf{at}mail.nih.gov.
Submitted on April 28, 2007
Revised on June 15, 2007
Accepted on 22 June 2007
Ferritin is a symmetric, 24-subunit iron-storage complex assembled of H and L chains. It is found in bacteria, plants and animals, and two classes of mutations in the human L-chain gene result in hereditary hyperferritinemia cataract syndrome or in neuroferritinopathy. Here, we examined systemic and cellular ferritin regulation and trafficking in the model organism Drosophila melanogaster. We showed that ferritin H and L transcripts are co-expressed during embryogenesis and that both subunits are essential for embryonic development. Ferritin overexpression impaired the survival of iron-deprived flies. In vivo expression of GFP-tagged holoferritin confirmed that iron-loaded ferritin molecules traffic through the Golgi organelle and are secreted into hemolymph. A constant ratio of ferritin H and L subunits, secured via tight post-transcriptional regulation, is characteristic of the secreted ferritin in flies. Differential cellular expression, conserved post-transcriptional regulation via the iron regulatory element, and distinct subcellular localization of the ferritin subunits prior to the assembly of holoferritin are all important steps mediating iron homeostasis. Our study revealed both conserved features and insect-specific adaptations of ferritin nanocages and provides novel imaging possibilities for their in vivo characterization.
Key Words: GFP, Golgi, iron metabolism, iron regulatory protein, secreted ferritin
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