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MBC in Press, published online ahead of print August 17, 2005
Mol. Biol. Cell 10.1091/mbc.E05-02-0159

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Submitted on February 24, 2005
Revised on August 9, 2005
Accepted on August 10, 2005

A Role for Fis1 in Both Mitochondrial and Peroxisomal Fission in Mammalian Cells

Annett Koch,* Yisang Yoon,{dagger} Nina A. Bonekamp,* Mark A. McNiven,{ddagger} and Michael Schrader*

*Department of Cell Biology and Cell Pathology, University of Marburg, 35037 Marburg, Germany; {dagger}Department of Anesthesiology, Pharmacology and Physiology, University of Rochester School of Medicine and Dentistry, Rochester, NY 14642; {ddagger}Department of Biochemistry and Molecular Biology, Mayo Clinic, Rochester, MN 55905

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 domaine 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 siRNA 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.

Address correspondence to: Michael Schrader (schrader{at}mailer.uni-marburg.de)




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