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Vol. 16, Issue 11, 5077-5086, November 2005
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* Department of Cell Biology and Cell Pathology, University of Marburg, 35037 Marburg, Germany;
Department of Anesthesiology, Pharmacology, and Physiology, University of Rochester School of Medicine and Dentistry, Rochester, NY 14642; and
Department of Biochemistry and Molecular Biology, Mayo Clinic, Rochester, MN 55905
Submitted February 24, 2005;
Revised August 9, 2005;
Accepted August 10, 2005
Monitoring Editor: Janet Shaw
The mammalian dynamin-like protein DLP1/Drp1 has been shown to mediate both mitochondrial and peroxisomal fission. In this study, we have examined whether hFis1, a mammalian homologue of yeast Fis1, which has been shown to participate in mitochondrial fission by an interaction with DLP1/Drp1, is also involved in peroxisomal growth and division. We show that hFis1 localizes to peroxisomes in addition to mitochondria. Through differential tagging and deletion experiments, we demonstrate that the transmembrane domain and the short C-terminal tail of hFis1 is both necessary and sufficient for its targeting to peroxisomes and mitochondria, whereas the N-terminal region is required for organelle fission. hFis1 promotes peroxisome division upon ectopic expression, whereas silencing of Fis1 by small interfering RNA inhibited fission and caused tubulation of peroxisomes. These findings provide the first evidence for a role of Fis1 in peroxisomal fission and suggest that the fission machinery of mitochondria and peroxisomes shares common components.
Abbreviations used: GFP, green fluorescent protein; PMP, peroxisomal membrane protein; TPR, tetratricopeptide repeat; YFP, yellow fluorescent protein.
The online version of this article contains supplemental material at MBC Online (http://www.molbiolcell.org).
Address correspondence to: Michael Schrader (schrader{at}mailer.uni-marburg.de).
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