A role for Fis1 in both mitochondrial and peroxisomal fission in mammalian cells
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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.
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DLP-1 has a shared function in peroxisomal and mitochondrial fission and is recruited to peroxisomes by MFF and FIS1 following PEX11β-mediated elongation.
“DLP-1 has a shared function in peroxisomal and mitochondrial fission, and is recruited to peroxisomes by two mitochondrial-associated fission factors, mitochondrial fission factor (MFF) (Gandre-Babbe and van der Bliek, 2008), and mitochondrial fission 1 (FIS1), following PEX11β-mediated elongation (Koch et al., 2005; Itoyama et al., 2013).”
From The cell biology of the retinal pigment epithelium (2020) · cites this paper as Koch et al., 2005
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- Authors
- Koch, A., Yoon, Y., Bonekamp, N. A., McNiven, M. A., & Schrader, M.
- Affiliations
- Philipps University of Marburg (DE)
- University of Rochester Medicine (US)
- Mayo Clinic (US)
- Venue
- Molecular Biology of the Cell
- Published
- 2005-11
- Volume
- 16
- Issue
- 11
- Pages
- 5077-5086
- ISSN
- 1059-1524 (ISSN-L)
- 1939-4586
- PMC
- PMC1266408
- OpenAlex
- W2128023952
- Cited by
- 308
- References
- 42
- Citations by year
- 2026: 8 · 2025: 8 · 2024: 13 · 2023: 13 · 2022: 16 · 2021: 8 · 2020: 17 · 2019: 10 · 2018: 17 · 2017: 11 · 2016: 15 · 2015: 17 · 2014: 14 · 2013: 24 · 2012: 15
- FWCI
- 6.42
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Molecular Biology of the Cell (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Philipps-Universität Marburg
- La Trobe University
- Universität Heidelberg
- Université de Genève
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Keywords
- Fis1, mitochondrial fission, Drp1, dynamin-like protein, peroxisome division, peroxisome targeting, transmembrane domain, C-terminal tail, mammalian cells
- MeSH terms
- Animals, Chlorocebus aethiops, Humans, Membrane Proteins, Microtubule-Associated Proteins, Mitochondria, Transfection, COS Cells, GTP Phosphohydrolases, Peroxisomes, Mitochondrial Proteins, Dynamins, RNA, Small Interfering, Cell Line, Tumor, Rats
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