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J. Biol. Chem., Vol. 278, Issue 50, 50142-50150, December 12, 2003
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Structure, Function, and Regulation of a Subfamily of Mouse Zinc Transporter Genes*
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From the
Department of Biochemistry and Molecular Biology, University of Kansas Medical Center, Kansas City, Kansas 66160-7421 and the ¶Departments of Nutritional Sciences and Biochemistry, University of Missouri, Columbia, Missouri 65211
Zinc is an essential metal for all eukaryotes, and cells have evolved a complex system of proteins to maintain the precise balance of zinc uptake, intracellular storage, and efflux. In mammals, zinc uptake appears to be mediated by members of the Zrt/Irt-like protein (ZIP) superfamily of metal ion transporters. Herein, we have studied a subfamily of zip genes (zip1, zip2, and zip3) that is conserved in mice and humans. These eight-transmembrane domain proteins contain a conserved 12-amino acid signature sequence within the fourth transmembrane domain. All three of these mouse ZIP proteins function to specifically increase the uptake of zinc in transfected cultured cells, similar to the previously demonstrated functions of human ZIP1 and ZIP2 (Gaither, L. A., and Eide, D. J. (2000) J. Biol. Chem. 275, 5560–5564; Gaither, L. A., and Eide, D. J. (2001) J. Biol. Chem. 276, 22258–22264). No ZIP3 orthologs have been previously studied. Furthermore, this first systematic comparative study of the in vivo expression and dietary zinc regulation of this subfamily of zip genes revealed that 1) zip1 mRNA is abundant in many mouse tissues, whereas zip2 and zip3 mRNAs are very rare or moderately rare, respectively, and tissue-restricted in their accumulation; and 2) unlike mouse metallothionein I and zip4 mRNAs (Dufner-Beattie, J., Wang, F., Kuo, Y.-M., Gitschier, J., Eide, D., and Andrews, G. K. (2003) J. Biol. Chem. 278, 33474–33481), the abundance of zip1, zip2, and zip3 mRNAs is not regulated by dietary zinc in the intestine and visceral endoderm, tissues involved in nutrient absorption. These studies suggest that all three of these ZIP proteins may play cell-specific roles in zinc homeostasis rather than primary roles in the acquisition of dietary zinc.
Received for publication, April 21, 2003 , and in revised form, July 15, 2003.
* This work was supported in part by National Institutes of Health Grants DK50181 (to G. K. A.) and GM56285 (to D. E.) and by pilot project funds from the University of Kansas Research Institute. 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.
Present address: Washington University School of Medicine, St. Louis, MO 63110.
|| To whom correspondence should be addressed: Dept. of Biochemistry and Molecular Biology, University of Kansas Medical Center, Mail Stop 3030, 39th and Rainbow Blvd., Kansas City, KS 66160-7421. Tel.: 913-588-6935; Fax: 913-588-2711; E-mail: gandrews{at}kumc.edu.
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