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J. Biol. Chem., Vol. 283, Issue 45, 31107-31115, November 7, 2008

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Targeting of hFis1 to Peroxisomes Is Mediated by Pex19p^*

Hannah K. Delille and Michael Schrader¹

From the Centre for Cell Biology and Department of Biology, University of Aveiro, Campus Universitário de Santiago, Aveiro 3810-193, Portugal and the Department of Cell Biology and Cell Pathology, University of Marburg, Marburg 35037, Germany

The processes of peroxisome formation and proliferation are still a matter of debate. We have previously shown that peroxisomes share some components of their division machinery with mitochondria. hFis1, a tail-anchored membrane protein, regulates the membrane fission of both organelles by DLP1/Drp1 recruitment, but nothing is known about the mechanisms of the dual targeting of hFis1. Here we demonstrate for the first time that peroxisomal targeting of hFis1 depends on Pex19p, a peroxisomal membrane protein import factor. hFis1/Pex19p binding was demonstrated by expression and co-immunoprecipitation studies. Using mutated versions of hFis1 an essential binding region for Pex19p was located within the last 26 C-terminal amino acids of hFis1, which are required for proper targeting to both mitochondria and peroxisomes. The basic amino acids in the very C terminus are not essential for Pex19p binding and peroxisomal targeting, but are instead required for mitochondrial targeting. Silencing of Pex19p by small interference RNA reduced the targeting of hFis1 to peroxisomes, but not to mitochondria. In contrast, overexpression of Pex19p alone was not sufficient to shift the targeting of hFis1 to peroxisomes. Our findings indicate that targeting of hFis1 to peroxisomes and mitochondria are independent events and support a direct, Pex19p-dependent targeting of peroxisomal tail-anchored proteins.

Received for publication, May 1, 2008 , and in revised form, September 3, 2008.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EBI Data Bank with accession number(s) NM_003847 [GenBank] and NM_002857 [GenBank] .

^* This work was supported by the German Research Foundation (Grant SCHR 518/6-1,2), the Portuguese Foundation for Science and Technology (Grant PTDC/BIA-BCM/71932/2006), and the University of Aveiro. 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.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Figs. S1 and S2.

¹ To whom correspondence should be addressed: Tel.: 351-234-370-200 (ext. 22789); Fax: 351-234-372-587; E-mail: mschrader{at}ua.pt.

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