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J. Biol. Chem., Vol. 280, Issue 1, 787-795, January 7, 2005

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Drosophila fear of intimacy Encodes a Zrt/IRT-like Protein (ZIP) Family Zinc Transporter Functionally Related to Mammalian ZIP Proteins^*

Wendy R. Mathews, Fudi Wang¶, David J. Eide||, and Mark Van Doren**

From the Department of Biology, Johns Hopkins University, Baltimore, Maryland 21218 and the Departments of Nutritional Sciences and Biochemistry, University of Missouri, Columbia, Missouri 65211

Zinc is essential for many cellular processes, and its concentration in the cell must be tightly controlled. The Zrt/IRT-like protein (ZIP) family of zinc transporters have recently been identified as the main regulators of zinc influx into the cytoplasm (1); however, little is known about their in vivo roles. Previously, we have shown that fear of intimacy (foi) encodes a putative member of the ZIP family that is essential for development in Drosophila (2). Here we demonstrate that FOI can act as an ion transporter in both yeast and mammalian cell assays and is specific for zinc. We also provide insight into the mechanism of action of the ZIP family through membrane topology and structure-function analyses of FOI. Our work demonstrates that Drosophila FOI is closely related to mammalian ZIP proteins at the functional level and that Drosophila represents an ideal system for understanding the in vivo roles of this family. In addition, this work indicates that the control of zinc by ZIP transporters may play a critical role in regulating developmental processes.

Received for publication, October 4, 2004

^* This work was supported by Grants GM56285 (to D. J. E.) and GM63023 (to M. V. D.) from the National Institutes of Health and by a grant from the Pew Charitable Trust (to M. V. D.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

^¶ Current address: Children's Hospital, Howard Hughes Medical Institute, Harvard Medical School, Boston, MA 02115.

^|| Current address: Dept. of Nutritional Sciences, University of Wisconsin-Madison, Madison, WI 53706.

^** To whom correspondence should be addressed: Dept. of Biology, 302 Mudd Hall, Johns Hopkins University, 3400 N. Charles St. Baltimore, MD 21218. Tel.: 410-516-4717; Fax: 410-516-5213; E-mail: vandoren{at}jhu.edu.

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