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© The Rockefeller University Press, 0021-9525/1997//895 $5.00
The Journal of Cell Biology, Volume 139, Number 4, , 1997 895-905

Article

Functional Expression Cloning and Characterization of SFT, a Stimulator of Fe Transport



Jesus A. Gutierrez, Jianming Yu, Susan Rivera, and Marianne Wessling-Resnick

Department of Nutrition, Harvard School of Public Health, Boston, Massachusetts 02115

A stimulator of Fe transport (SFT) was identified by functional expression cloning in Xenopus oocytes. SFT-mediated transport has properties defined for transferrin-independent Fe uptake, but its cytolocalization in recycling endosomes and the observed stimulation of transferrin-bound Fe assimilation indicate a key role in intracellular Fe membrane transport as well. SFT has six predicted transmembranous domains and a functionally important RExxE motif that resembles domains involved in yeast Fe transport and Fe-binding by ferritin L-chains. The observation that SFT oligomerizes, along with other structural and mechanistic features, suggests it may be a member of either the ATP-binding cassette or cation diffusion facilitator families. The 3' untranslated region of SFT contains a translation inhibitory element and inhibition of SFT expression in Xenopus oocytes was found to be relieved by coinjection of transcripts from other defined cDNAs that are also described in this report. SFT is the first component of the mammalian Fe membrane transport machinery to be identified.

Abbreviations used in this paper: ABC, ATP-binding cassette; ACADM, acyl co-A dehydrogenase; GFP, green fluorescent protein; NTA, nitriloacetic acid; ORF, open reading frame; PMA, phorbol 12-myristate 13-acetate; SFT, stimulator of Fe transport; Tf, transferrin; TIE, translation inhibitory element; UTR, untranslated region; XFGFR, Xenopus FGF receptor.

The authors are indebted to A.H. Tashjian and B. Han (Harvard School of Public Health, Boston, MA) for providing use of Xenopus laevis facilities and microinjection equipment as well as their kind advice and scientific input. A special note of appreciation also goes to W. Boll and T. Kirchhausen (Harvard Medical School, Boston, MA) who kindly provided intrumentation, expertise, and advice for the fluorescence microscopy experiments. The Harvard School of Public Health Biostastics Consulting Laboratory, and in particular, C. Corcoran, C. Wagner, and S. Kim, are gratefully acknowledged for their assistance. We also appreciate the advice of E. Hartmann (Max Delbruck Center, Berlin, Germany) in transmembrane structure prediction.

J.A. Gutierrez and J. Yu contributed equally to this paper.

Address all correspondence to M. Wessling-Resnick, Department of Nutrition, Harvard School of Public Health, 665 Huntington Avenue, Boston, MA 02115. Tel.: (617) 432-3267. Fax: (617) 432-2435.

J.A. Gutierrez's present address is Elanco Animal Health Research and Development, 2001 W. Main Street, P.O. Box 708, Greenfield, IN 46140.


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