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Blood, 1 March 2007, Vol. 109, No. 5, pp. 2205-2209. Prepublished online as a Blood First Edition Paper on October 31, 2006; DOI 10.1182/blood-2006-06-032516. This Article Full Text Full Text (PDF) All Versions of this Article: blood-2006-06-032516v1 109/5/2205    most recent Alert me when this article is cited Alert me if a correction is posted Citation Map 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 Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by De Domenico, I. Articles by Kaplan, J. Search for Related Content PubMed PubMed Citation Articles by De Domenico, I. Articles by Kaplan, J. Related Collections Red Cells Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  RED CELLS Evidence for the multimeric structure of ferroportin Ivana De Domenico1, Diane McVey Ward1, Giovanni Musci2, and Jerry Kaplan1 1 Department of Pathology, School of Medicine, University of Utah, Salt Lake City; 2 Dipartimento di Scienze e Tecnologie Agro-alimentari Ambientali e Microbiologiche, Università del Molise, Italy Ferroportin (Fpn) (IREG1, SLC40A1, MTP1) is an iron transporter, and mutations in Fpn result in a genetically dominant form of iron overload disease. Previously, we demonstrated that Fpn is a multimer and that mutations in Fpn are dominant negative. Other studies have suggested that Fpn is not a multimer and that overexpression or epitope tags might affect the localization, topology, or multimerization of Fpn. We generated wild-type Fpn with 3 different epitopes, GFP, FLAG, and c-myc, and expressed these constructs in cultured cells. Co-expression of any 2 different epitope-tagged proteins in the same cell resulted in their quantitative coimmunoprecipitation. Treatment of Fpn-GFP/Fpn-FLAG–expressing cells with crosslinking reagents resulted in the crosslinking of Fpn-GFP and Fpn-FLAG. Western analysis of rat glioma C6 cells or mouse bone marrow macrophages exposed to crosslinking reagents showed that endogenous Fpn is a dimer. These results support the hypothesis that the dominant inheritance of Fpn–iron overload disease is due to the dominant-negative effects of mutant Fpn proteins. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: I. De Domenico, E. Lo, D. M. Ward, and J. Kaplan Hepcidin-induced internalization of ferroportin requires binding and cooperative interaction with Jak2 PNAS, March 10, 2009; 106(10): 3800 - 3805. [Abstract] [Full Text] [PDF] K.-y. Yeh, M. Yeh, L. Mims, and J. Glass Iron feeding induces ferroportin 1 and hephaestin migration and interaction in rat duodenal epithelium Am J Physiol Gastrointest Liver Physiol, January 1, 2009; 296(1): G55 - G65. [Abstract] [Full Text] [PDF] I. De Domenico, M. B. Vaughn, D. Yoon, J. P. Kushner, D. M. Ward, and J. Kaplan Zebrafish as a model for defining the functional impact of mammalian ferroportin mutations Blood, November 15, 2007; 110(10): 3780 - 3783. [Abstract] [Full Text] [PDF] X. S. Liu, L. D. Patterson, M. J. Miller, and E. C. Theil Peptides Selected for the Protein Nanocage Pores Change the Rate of Iron Recovery from the Ferritin Mineral J. Biol. Chem., November 2, 2007; 282(44): 31821 - 31825. [Abstract] [Full Text] [PDF] I. De Domenico, D. M. Ward, C. Langelier, M. B. Vaughn, E. Nemeth, W. I. Sundquist, T. Ganz, G. Musci, and J. Kaplan The Molecular Mechanism of Hepcidin-mediated Ferroportin Down-Regulation Mol. Biol. Cell, July 1, 2007; 18(7): 2569 - 2578. [Abstract] [Full Text] [PDF] I. E. Zohn, I. De Domenico, A. Pollock, D. M. Ward, J. F. Goodman, X. Liang, A. J. Sanchez, L. Niswander, and J. Kaplan The flatiron mutation in mouse ferroportin acts as a dominant negative to cause ferroportin disease Blood, May 15, 2007; 109(10): 4174 - 4180. [Abstract] [Full Text] [PDF]

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