- THIS ARTICLE
- Full Text
- Full Text (PDF)
- Data Supplement
-
All Versions of this Article:
genetics.107.075150v1
177/1/89 most recent - Alert me when this article is cited
- Alert me if a correction is posted
- SERVICES
- Email this article to a friend
- Similar articles in this journal
- Similar articles in PubMed
- Alert me to new issues of the journal
- Download to citation manager
- Reprints & Permissions
- CITING ARTICLES
- Citing Articles via HighWire
- Citing Articles via Google Scholar
- GOOGLE SCHOLAR
- Articles by Missirlis, F.
- Articles by Rouault, T. A.
- Search for Related Content
- PUBMED
- PubMed Citation
- Articles by Missirlis, F.
- Articles by Rouault, T. A.
Originally published as Genetics Published Articles Ahead of Print on July 1, 2007.
Genetics, Vol. 177, 89-100, September 2007, Copyright © 2007
doi:10.1534/genetics.107.075150
Homeostatic Mechanisms for Iron Storage Revealed by Genetic Manipulations and Live Imaging of Drosophila Ferritin
Fanis Missirlis*,1,
Stylianos Kosmidis
,
Tom Brody
,
Manos Mavrakis*,
Sara Holmberg*,
Ward F. Odenwald,
Efthimios M. C. Skoulakis and
Tracey A. Rouault*
* Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, Bethesda, Maryland 20892, Institute of Molecular Biology and Genetics BSRC "Alexander Fleming," Vari, 16672, Greece and Neural Cell-Fate Determinants Section, National Institute of Neurological Disorders and Stroke, Bethesda, Maryland 20892
1 Corresponding author: National Institutes of Health, Bldg. 18T, Room 101, 9000 Rockville Pike, Bethesda, MD 20892.
E-mail: missirlf{at}mail.nih.gov
Ferritin is a symmetric, 24-subunit iron-storage complex assembled of H and L chains. It is found in bacteria, plants, and animals and in two classes of mutations in the human L-chain gene, resulting 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 coexpressed 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.
This article has been cited by other articles:
 |
|
 |
|
  O. Hajdusek, D. Sojka, P. Kopacek, V. Buresova, Z. Franta, I. Sauman, J. Winzerling, and L. Grubhoffer Knockdown of proteins involved in iron metabolism limits tick reproduction and development PNAS, January 27, 2009; 106(4): 1033 - 1038. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
G. Chamilos, R. E. Lewis, J. Hu, L. Xiao, T. Zal, M. Gilliet, G. Halder, and D. P. Kontoyiannis Drosophila melanogaster as a model host to dissect the immunopathogenesis of zygomycosis PNAS, July 8, 2008; 105(27): 9367 - 9372. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 H. Shi, K. Z. Bencze, T. L. Stemmler, and C. C. Philpott A Cytosolic Iron Chaperone That Delivers Iron to Ferritin Science, May 30, 2008; 320(5880): 1207 - 1210. [Abstract] [Full Text] [PDF]
|
|