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J. Biol. Chem., Vol. 280, Issue 23, 22181-22190, June 10, 2005

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Post-transcriptional Regulation of the Yeast High Affinity Iron Transport System^*

M. Rosa Felice, Ivana De Domenico¶, Liangtao Li¶, Diane McVey Ward¶, Beatrix Bartok¶, Giovanni Musci, and Jerry Kaplan¶||

From the Dipartimento di Scienze Microbiologiche Genetiche e Molecolari, Università di Messina, Salita Sperone 31, I-98166 Villaggio S. Agata, Messina I-98166, Italia and the ^¶Division of Immunology and Cell Biology, Department of Pathology, School of Medicine, University of Utah, Salt Lake City, Utah 84132

Saccharomyces cerevisiae transcriptionally regulates the expression of the plasma membrane high affinity iron transport system in response to iron need. This transport system is comprised of the products of the FET3 and FTR1 genes. We show that Fet3p and Ftr1p are post-translationally regulated by iron. Incubation of cells in high iron leads to the internalization and degradation of both Fet3p and Ftr1p. Yeast strains defective in endocytosis (end4) show a reduced iron-induced loss of Fet3p-Ftr1p. In cells with a deletion in the vacuolar protease PEP4, high iron medium leads to the accumulation of Fet3p and Ftr1p in the vacuole. Iron-induced degradation of Fet3p-Ftr1p is significantly reduced in strains containing a deletion of a gene, VTA1, which is involved in multivesicular body (MVB) sorting in yeast. Sorting through the MVB can involve ubiquitination. We demonstrate that Ftr1p is ubiquitinated, whereas Fet3p is not ubiquitinated. Iron-induced internalization and degradation of Fet3p-Ftr1p occurs in a mutant strain of the E3 ubiquitin ligase RSP5 (rsp5-1), suggesting that Rsp5p is not required. Internalization of Fet3p-Ftr1p is specific for iron and requires both an active Fet3p and Ftr1p, indicating that it is the transport of iron through the iron permease Ftr1p that is responsible for the internalization and degradation of the Fet3p-Ftr1p complex.

Received for publication, December 29, 2004 , and in revised form, March 21, 2005.

^* This work was supported by National Institutes of Health Grant DK30534. Support for DNA oligonucleotides and sequencing was provided by Cancer Center Support Grant CA43014. 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.

Both authors contributed equally to this work.

^|| To whom correspondence should be addressed: Dept. of Pathology, School of Medicine, University of Utah, 50 N. Medical Dr., Salt Lake City, UT 84132. Tel.: 801-581-7427; Fax: 801-581-4517; E-mail: jerry.kaplan{at}path.utah.edu.

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